2jvy - Revision history

OCA at 13:07, 26 July 2023

OCA — Wed, 26 Jul 2023 13:07:27 GMT

←Older revision		Revision as of 13:07, 26 July 2023
Line 1:		Line 1:

	==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==		==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==
-	<StructureSection load='2jvy' size='340' side='right'caption='[[2jvy~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='2jvy' size='340' side='right'caption='[[2jvy]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JVY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JVY FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2jvx\|2jvx]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [https://pdbe.org/2jvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [https://www.ebi.ac.uk/pdbsum/2jvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvy ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [https://pdbe.org/2jvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [https://www.ebi.ac.uk/pdbsum/2jvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[https://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref> <ref>PMID:16547522</ref> <ref>PMID:21606507</ref> <ref>PMID:19185524</ref> <ref>PMID:11047757</ref> <ref>PMID:11242109</ref> <ref>PMID:11224521</ref> <ref>PMID:12045264</ref> <ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[https://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[https://omim.org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref> <ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[https://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref> <ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[https://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[https://omim.org/entry/308300 308300]]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref> <ref>PMID:17728323</ref> <ref>PMID:19185524</ref> <ref>PMID:16950813</ref> <ref>PMID:10839543</ref> <ref>PMID:19033441</ref> <ref>PMID:11590134</ref> <ref>PMID:15229184</ref>	+	[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[https://omim.org/entry/300291 300291]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref> <ref>PMID:16547522</ref> <ref>PMID:21606507</ref> <ref>PMID:19185524</ref> <ref>PMID:11047757</ref> <ref>PMID:11242109</ref> <ref>PMID:11224521</ref> <ref>PMID:12045264</ref> <ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[https://omim.org/entry/300301 300301]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[https://omim.org/entry/300584 300584]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref> <ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[https://omim.org/entry/300636 300636]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref> <ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[https://omim.org/entry/300640 300640]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[https://omim.org/entry/308300 308300]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref> <ref>PMID:17728323</ref> <ref>PMID:19185524</ref> <ref>PMID:16950813</ref> <ref>PMID:10839543</ref> <ref>PMID:19033441</ref> <ref>PMID:11590134</ref> <ref>PMID:15229184</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref> <ref>PMID:19854139</ref> <ref>PMID:20724660</ref>	+	[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref> <ref>PMID:19854139</ref> <ref>PMID:20724660</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Agou, F]]	+	[[Category: Agou F]]
-	[[Category: Cordier, F]]	+	[[Category: Cordier F]]
-	[[Category: Delepierre, M]]	+	[[Category: Delepierre M]]
-	[[Category: Veron, M]]	+	[[Category: Veron M]]
-	[[Category: Vinolo, E]]	+	[[Category: Vinolo E]]
-	~~[[Category: Beta-beta-alpha fold]]~~	+
-	~~[[Category: Cchc classical zinc finger]]~~	+
-	~~[[Category: Cchf mutant zinc finger]]~~	+
-	~~[[Category: Coiled coil]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Ectodermal dysplasia]]~~	+
-	~~[[Category: Eda-id c417f mutant of nemo zinc finger]]~~	+
-	~~[[Category: Host-virus interaction]]~~	+
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation~~]]	+

OCA at 17:59, 20 October 2021

OCA — Wed, 20 Oct 2021 17:59:07 GMT

OCA at 06:51, 19 February 2020

OCA — Wed, 19 Feb 2020 06:51:06 GMT

←Older revision		Revision as of 06:51, 19 February 2020
Line 1:		Line 1:

	==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==		==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==
-	<StructureSection load='2jvy' size='340' side='right' caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='2jvy' size='340' side='right'caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JVY FirstGlance]. <br>		<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JVY FirstGlance]. <br>
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Agou, F]]		[[Category: Agou, F]]
	[[Category: Cordier, F]]		[[Category: Cordier, F]]

OCA at 11:15, 18 July 2018

OCA — Wed, 18 Jul 2018 11:15:01 GMT

←Older revision		Revision as of 11:15, 18 July 2018
Line 1:		Line 1:
		+
	==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==		==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==
	<StructureSection load='2jvy' size='340' side='right' caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2jvy' size='340' side='right' caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [http://pdbe.org/2jvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [http://www.ebi.ac.uk/pdbsum/2jvy PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [http://pdbe.org/2jvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [http://www.ebi.ac.uk/pdbsum/2jvy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 32:		Line 33:
	[[Category: Cchc classical zinc finger]]		[[Category: Cchc classical zinc finger]]
	[[Category: Cchf mutant zinc finger]]		[[Category: Cchf mutant zinc finger]]
		+	[[Category: Coiled coil]]
		+	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Ectodermal dysplasia]]		[[Category: Ectodermal dysplasia]]

OCA at 02:54, 10 September 2015

OCA — Thu, 10 Sep 2015 02:54:33 GMT

←Older revision		Revision as of 02:54, 10 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [http://www.ebi.ac.uk/pdbsum/2jvy PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [http://pdbe.org/2jvy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [http://www.ebi.ac.uk/pdbsum/2jvy PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2jvy" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:49, 18 December 2014

OCA — Thu, 18 Dec 2014 12:49:53 GMT

←Older revision		Revision as of 12:49, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}~~	+	==Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger==
-	===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===	+	<StructureSection load='2jvy' size='340' side='right' caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_18313693}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JVY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [http://www.ebi.ac.uk/pdbsum/2jvy PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[http://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref> <ref>PMID:16547522</ref> <ref>PMID:21606507</ref> <ref>PMID:19185524</ref> <ref>PMID:11047757</ref> <ref>PMID:11242109</ref> <ref>PMID:11224521</ref> <ref>PMID:12045264</ref> <ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[http://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[http://omim.org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref> <ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[http://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref> <ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[http://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[http://omim.org/entry/308300 308300]]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref> <ref>PMID:17728323</ref> <ref>PMID:19185524</ref> <ref>PMID:16950813</ref> <ref>PMID:10839543</ref> <ref>PMID:19033441</ref> <ref>PMID:11590134</ref> <ref>PMID:15229184</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref> <ref>PMID:19854139</ref> <ref>PMID:20724660</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The regulatory NEMO (NF-kappaB essential modulator) protein has a crucial role in the canonical NF-kappaB signaling pathway notably involved in immune and inflammatory responses, apoptosis and oncogenesis. The regulatory domain is located in the C-terminal half of NEMO and contains a classical CCHC-type zinc finger (ZF). We have investigated the structural and functional effects of a cysteine to phenylalanine point mutation (C417F) in the ZF motif, identified in patients with anhidrotic ectodermal dysplasia with immunodeficiency. The solution structures of the wild type and mutant ZF were determined by NMR. Remarkably, the mutant adopts a global betabetaalpha fold similar to that of the wild type and retains thermodynamic stability, i.e., the ability to bind zinc with a native-like affinity, although the last zinc-chelating residue is missing. However, the mutation induces enhanced dynamics in the motif and leads to an important loss of stability. A detailed analysis of the wild type solution structure and experimental evidences led to the identification of two possible protein-binding surfaces that are largely destabilized in the mutant. This is sufficient to alter NEMO function, since functional complementation assays using NEMO-deficient pre-B and T lymphocytes show that full-length C417F pathogenic NEMO leads to a partial to strong defect in LPS, IL-1beta and TNF-alpha-induced NF-kappaB activation, respectively, as compared to wild type NEMO. Altogether, these results shed light onto the role of NEMO ZF as a protein-binding motif and show that a precise structural integrity of the ZF should be preserved to lead to a functional protein-recognition motif triggering full NF-kappaB activation.

-	~~==Disease==~~	+	Solution Structure of NEMO Zinc Finger and Impact of an Anhidrotic Ectodermal Dysplasia with Immunodeficiency-related Point Mutation.,Cordier F, Vinolo E, Veron M, Delepierre M, Agou F J Mol Biol. 2008 Jan 30;. PMID:18313693<ref>PMID:18313693</ref>
-	~~[[http://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause~~ of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[http://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref><ref>PMID:16547522</ref><ref>PMID:21606507</ref><ref>PMID:19185524</ref><ref>PMID:11047757</ref><ref>PMID:11242109</ref><ref>PMID:11224521</ref><ref>PMID:12045264</ref><ref>PMID:15100680</ref> Defects in IKBKG are the cause of ~~ectodermal dysplasia anhidrotic~~ with ~~immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[http://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO~~-related ~~without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[http://omim~~.~~org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia~~, ~~isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities~~, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref><ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[http://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, ~~such as bacillus Calmette-Guerin vaccines and non-tuberculous~~, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref><ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[http://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, ~~whether caused by the same or different serotypes or strains~~. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[http://omim.org/entry/308300 308300]]; ~~formerly designed familial incontinentia pigmenti type II (IP2)~~. IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:~~20010814</ref><ref>PMID:17728323</ref><ref>PMID:19185524</ref><ref>PMID:16950813</ref><ref>PMID:10839543</ref><ref>PMID:19033441</ref><ref>PMID:11590134</ref>~~<ref>PMID:~~15229184~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~//www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, ~~the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be~~ a ~~mediator for TAX activation~~ of ~~NF-kappa-B~~. ~~Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity)~~. ~~Essential for viral activation~~ of ~~IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination~~.<~~ref~~>~~PMID:14695475~~</~~ref~~>~~<ref>PMID:19854139</ref><ref>PMID:20724660</ref>~~	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	~~[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA].~~	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+	[[Category: Agou, F]]
-	~~<ref group="xtra">PMID:018313693</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	[[Category: Cordier, F]]
-	[[Category: Agou, F.]]	+	[[Category: Delepierre, M]]
-	[[Category: Cordier, F.]]	+	[[Category: Veron, M]]
-	[[Category: Delepierre, M.]]	+	[[Category: Vinolo, E]]
-	[[Category: Veron, M.]]	+
-	[[Category: Vinolo, E.]]	+
	[[Category: Beta-beta-alpha fold]]		[[Category: Beta-beta-alpha fold]]
	[[Category: Cchc classical zinc finger]]		[[Category: Cchc classical zinc finger]]

OCA at 21:26, 24 March 2013

OCA — Sun, 24 Mar 2013 21:26:21 GMT

←Older revision		Revision as of 21:26, 24 March 2013
Line 1:		Line 1:
-	[[Image:2jvy.png\|left\|200px]]
-
	{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}		{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}
-
	===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===		===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===
		+	{{ABSTRACT_PUBMED_18313693}}

-	~~{{ABSTRACT_PUBMED_18313693}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[http://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref><ref>PMID:16547522</ref><ref>PMID:21606507</ref><ref>PMID:19185524</ref><ref>PMID:11047757</ref><ref>PMID:11242109</ref><ref>PMID:11224521</ref><ref>PMID:12045264</ref><ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[http://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[http://omim.org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref><ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[http://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref><ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[http://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[http://omim.org/entry/308300 308300]]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref><ref>PMID:17728323</ref><ref>PMID:19185524</ref><ref>PMID:16950813</ref><ref>PMID:10839543</ref><ref>PMID:19033441</ref><ref>PMID:11590134</ref><ref>PMID:15229184</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref><ref>PMID:19854139</ref><ref>PMID:20724660</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018313693</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018313693</ref><references group="xtra"/><references/>
	[[Category: Agou, F.]]		[[Category: Agou, F.]]
	[[Category: Cordier, F.]]		[[Category: Cordier, F.]]

OCA: Protected "2jvy" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 14:41:54 GMT

Protected "2jvy" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:41, 7 January 2013

OCA at 14:41, 7 January 2013

OCA — Mon, 07 Jan 2013 14:41:52 GMT

←Older revision		Revision as of 14:41, 7 January 2013
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-	{{Seed}}
	[[Image:2jvy.png\|left\|200px]]		[[Image:2jvy.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2jvy", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}		{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}

	===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===		===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18313693}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18313693 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18313693}}		{{ABSTRACT_PUBMED_18313693}}

	==About this Structure==		==About this Structure==
-	~~2JVY is a~~ [[~~Single protein~~]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA].	+	[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA].

	==Reference==		==Reference==
-	Solution Structure of NEMO Zinc Finger and Impact of an Anhidrotic Ectodermal Dysplasia with Immunodeficiency-related Point Mutation., Cordier F, Vinolo E, Veron M, Delepierre M, Agou F, J Mol Biol. 2008 Jan 30;. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18313693 18313693]~~	+	<ref group="xtra">PMID:018313693</ref><references group="xtra"/>
-	~~[[Category: Single protein]]~~	+
	[[Category: Agou, F.]]		[[Category: Agou, F.]]
	[[Category: Cordier, F.]]		[[Category: Cordier, F.]]
Line 33:		Line 20:
	[[Category: Cchc classical zinc finger]]		[[Category: Cchc classical zinc finger]]
	[[Category: Cchf mutant zinc finger]]		[[Category: Cchf mutant zinc finger]]
-	[[Category: Coiled coil]]
-	[[Category: Cytoplasm]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Ectodermal dysplasia]]		[[Category: Ectodermal dysplasia]]
Line 43:		Line 28:
	[[Category: Transcription]]		[[Category: Transcription]]
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:36:58 2008''

OCA at 14:36, 27 July 2008

OCA — Sun, 27 Jul 2008 14:36:59 GMT

←Older revision		Revision as of 14:36, 27 July 2008
Line 1:		Line 1:
-	[[Image:2jvy.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2jvy.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}		{{STRUCTURE_2jvy\| PDB=2jvy \| SCENE= }}

-	~~'''~~Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger~~'''~~	+	===Solution Structure of the EDA-ID-related C417F mutant of human NEMO zinc finger===


-	~~==Overview==~~	+	<!--
-	~~The regulatory NEMO (NF~~-~~kappaB essential modulator) protein has a crucial role in the canonical NF~~-~~kappaB signaling pathway notably involved in immune and inflammatory responses, apoptosis and oncogenesis.~~ The regulatory domain is located in the C-terminal half of NEMO and contains a classical CCHC-type zinc finger (ZF). We have investigated the structural and functional effects of a cysteine to phenylalanine point mutation (C417F) in the ZF motif, ~~identified in patients with anhidrotic ectodermal dysplasia with immunodeficiency. The solution structures of the wild type and mutant ZF were determined by NMR. Remarkably~~, the ~~mutant adopts a global betabetaalpha fold similar~~ to ~~that of~~ the ~~wild type and retains thermodynamic stability, i~~.e., ~~the ability to bind zinc with a native-like affinity, although the last zinc-chelating residue~~ is ~~missing. However,~~ the ~~mutation induces enhanced dynamics in the motif and leads to an important loss of stability~~. ~~A detailed analysis of the wild type solution structure and experimental evidences led to the identification of two possible protein~~-~~binding surfaces that are largely destabilized in the mutant. This is sufficient to alter NEMO function, since functional complementation assays using NEMO~~-deficient pre-B and T lymphocytes show that full-length C417F pathogenic NEMO leads to a partial to strong defect in LPS, IL-1beta and TNF-alpha-induced NF-kappaB activation, respectively, as compared to wild type NEMO. Altogether, these results shed light onto the role of NEMO ZF as a protein-binding motif and show that a precise structural integrity of the ZF should be preserved to lead to a functional protein-recognition motif triggering full NF-kappaB activation.	+	The line below this paragraph, {{ABSTRACT_PUBMED_18313693}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18313693 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18313693}}

	==About this Structure==		==About this Structure==
-	2JVY is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA].	+	2JVY is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA].

	==Reference==		==Reference==
Line 39:		Line 43:
	[[Category: Transcription]]		[[Category: Transcription]]
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Apr 9 14~~:39:49 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:36:58 2008''

←Older revision		Revision as of 17:59, 20 October 2021
Line 3:		Line 3:
	<StructureSection load='2jvy' size='340' side='right'caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2jvy' size='340' side='right'caption='[[2jvy]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2JVY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2jvy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JVY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jvx\|2jvx]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jvx\|2jvx]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [~~http~~://pdbe.org/2jvy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2jvy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvy ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jvy OCA], [https://pdbe.org/2jvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jvy RCSB], [https://www.ebi.ac.uk/pdbsum/2jvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jvy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[~~http~~://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref> <ref>PMID:16547522</ref> <ref>PMID:21606507</ref> <ref>PMID:19185524</ref> <ref>PMID:11047757</ref> <ref>PMID:11242109</ref> <ref>PMID:11224521</ref> <ref>PMID:12045264</ref> <ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[~~http~~://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[~~http~~://omim.org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref> <ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[~~http~~://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref> <ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[~~http~~://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[~~http~~://omim.org/entry/308300 308300]]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref> <ref>PMID:17728323</ref> <ref>PMID:19185524</ref> <ref>PMID:16950813</ref> <ref>PMID:10839543</ref> <ref>PMID:19033441</ref> <ref>PMID:11590134</ref> <ref>PMID:15229184</ref>	+	[[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:[https://omim.org/entry/300291 300291]]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases.<ref>PMID:14651848</ref> <ref>PMID:16547522</ref> <ref>PMID:21606507</ref> <ref>PMID:19185524</ref> <ref>PMID:11047757</ref> <ref>PMID:11242109</ref> <ref>PMID:11224521</ref> <ref>PMID:12045264</ref> <ref>PMID:15100680</ref> Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:[https://omim.org/entry/300301 300301]]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:[https://omim.org/entry/300584 300584]]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases.<ref>PMID:15100680</ref> <ref>PMID:15356572</ref> Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:[https://omim.org/entry/300636 300636]]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of Mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis.<ref>PMID:19185524</ref> <ref>PMID:16818673</ref> Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:[https://omim.org/entry/300640 300640]]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD.<ref>PMID:16950813</ref> Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:[https://omim.org/entry/308300 308300]]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring.<ref>PMID:20010814</ref> <ref>PMID:17728323</ref> <ref>PMID:19185524</ref> <ref>PMID:16950813</ref> <ref>PMID:10839543</ref> <ref>PMID:19033441</ref> <ref>PMID:11590134</ref> <ref>PMID:15229184</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref> <ref>PMID:19854139</ref> <ref>PMID:20724660</ref>	+	[[https://www.uniprot.org/uniprot/NEMO_HUMAN NEMO_HUMAN]] Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity (By similarity). Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.<ref>PMID:14695475</ref> <ref>PMID:19854139</ref> <ref>PMID:20724660</ref>
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	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==