4p3w - Revision history

OCA at 07:10, 27 September 2023

OCA — Wed, 27 Sep 2023 07:10:53 GMT

←Older revision		Revision as of 07:10, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3W FirstGlance]. <br>		<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [https://pdbe.org/4p3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [https://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w 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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [https://pdbe.org/4p3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [https://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:40, 1 February 2023

OCA — Wed, 01 Feb 2023 12:40:27 GMT

←Older revision		Revision as of 12:40, 1 February 2023
Line 1:		Line 1:

	==Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide==		==Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide==
-	<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4p3w' size='340' side='right'caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4P3W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3W FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FLNA, FLN, FLN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [https://pdbe.org/4p3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [https://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [~~http~~://pdbe.org/4p3w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN]] Defects in FLNA are the cause of periventricular nodular heterotopia type 1 (PVNH1) [MIM:[~~http~~://omim.org/entry/300049 300049]]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH is a developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.<ref>PMID:16299064</ref> <ref>PMID:11532987</ref> <ref>PMID:12410386</ref> <ref>PMID:11914408</ref> <ref>PMID:15249610</ref> Defects in FLNA are the cause of periventricular nodular heterotopia type 4 (PVNH4) [MIM:[~~http~~://omim.org/entry/300537 300537]]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood. Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:[~~http~~://omim.org/entry/311300 311300]]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.<ref>PMID:12612583</ref> <ref>PMID:15940695</ref> Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:[~~http~~://omim.org/entry/304120 304120]]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:[~~http~~://omim.org/entry/305620 305620]]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.<ref>PMID:12612583</ref> <ref>PMID:16596676</ref> Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:[~~http~~://omim.org/entry/309350 309350]]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.<ref>PMID:12612583</ref> Defects in FLNA are the cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:[~~http~~://omim.org/entry/300048 300048]]. CIIPX is characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.<ref>PMID:17357080</ref> Defects in FLNA are the cause of FG syndrome type 2 (FGS2) [MIM:[~~http~~://omim.org/entry/300321 300321]]. FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.<ref>PMID:17632775</ref> Defects in FLNA are the cause of terminal osseous dysplasia (TOD) [MIM:[~~http~~://omim.org/entry/300244 300244]]. A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.<ref>PMID:20598277</ref> Defects in FLNA are the cause of cardiac valvular dysplasia X-linked (CVDX) [MIM:[~~http~~://omim.org/entry/314400 314400]]. A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.<ref>PMID:17190868</ref> Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abonormally enlarged.	+	[https://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN] Defects in FLNA are the cause of periventricular nodular heterotopia type 1 (PVNH1) [MIM:[https://omim.org/entry/300049 300049]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH is a developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.<ref>PMID:16299064</ref> <ref>PMID:11532987</ref> <ref>PMID:12410386</ref> <ref>PMID:11914408</ref> <ref>PMID:15249610</ref> Defects in FLNA are the cause of periventricular nodular heterotopia type 4 (PVNH4) [MIM:[https://omim.org/entry/300537 300537]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood. Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:[https://omim.org/entry/311300 311300]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.<ref>PMID:12612583</ref> <ref>PMID:15940695</ref> Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:[https://omim.org/entry/304120 304120]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:[https://omim.org/entry/305620 305620]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.<ref>PMID:12612583</ref> <ref>PMID:16596676</ref> Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:[https://omim.org/entry/309350 309350]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.<ref>PMID:12612583</ref> Defects in FLNA are the cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:[https://omim.org/entry/300048 300048]. CIIPX is characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.<ref>PMID:17357080</ref> Defects in FLNA are the cause of FG syndrome type 2 (FGS2) [MIM:[https://omim.org/entry/300321 300321]. FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.<ref>PMID:17632775</ref> Defects in FLNA are the cause of terminal osseous dysplasia (TOD) [MIM:[https://omim.org/entry/300244 300244]. A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.<ref>PMID:20598277</ref> Defects in FLNA are the cause of cardiac valvular dysplasia X-linked (CVDX) [MIM:[https://omim.org/entry/314400 314400]. A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.<ref>PMID:17190868</ref> Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abonormally enlarged.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN]] Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis.<ref>PMID:22121117</ref> [[http://www.uniprot.org/uniprot/FBLI1_HUMAN FBLI1_HUMAN]] Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion.<ref>PMID:12679033</ref> <ref>PMID:12496242</ref> <ref>PMID:18829455</ref> <ref>PMID:19074766</ref>	+	[https://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN] Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis.<ref>PMID:22121117</ref>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Pentikainen, U~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Seppala, J~~]]	+	[[Category: Pentikainen U]]
-	[[Category: ~~Ylanne,~~ J]]	+	[[Category: Seppala J]]
-	[[Category: ~~Actin binding protein]]~~	+	[[Category: Ylanne J]]
-	~~[[Category: Adhesion]]~~	+
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Immunoglobulin-like~~]]	+

OCA at 08:33, 22 November 2017

OCA — Wed, 22 Nov 2017 08:33:20 GMT

←Older revision		Revision as of 08:33, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FLNA, FLN, FLN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [http://pdbe.org/4p3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [http://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [http://pdbe.org/4p3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [http://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</span></td></tr>
	</table>		</table>
Line 15:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Pentikainen, U]]		[[Category: Pentikainen, U]]
	[[Category: Seppala, J]]		[[Category: Seppala, J]]

OCA at 16:04, 17 May 2017

OCA — Wed, 17 May 2017 16:04:50 GMT

←Older revision		Revision as of 16:04, 17 May 2017
Line 1:		Line 1:
		+
	==Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide==		==Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide==
	<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3W FirstGlance]. <br>		<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [http://www.ebi.ac.uk/pdbsum/4p3w 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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [http://pdbe.org/4p3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [http://www.ebi.ac.uk/pdbsum/4p3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3w ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 14:44, 12 August 2015

OCA — Wed, 12 Aug 2015 14:44:36 GMT

←Older revision		Revision as of 14:44, 12 August 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide==
-		+	<StructureSection load='4p3w' size='340' side='right' caption='[[4p3w]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~The entry~~ 4p3w is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4p3w]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3W FirstGlance]. <br>
-	~~Authors~~: ~~Seppala~~, J., ~~Pentikainen, U~~., ~~Ylanne, J~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p3w RCSB], [http://www.ebi.ac.uk/pdbsum/4p3w PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure~~ of the ~~human filamin A Ig~~-like ~~domains 20~~-21 in ~~complex~~ with ~~migfilin peptide~~	+	</table>
-	[[Category: ~~Unreleased Structures~~]]	+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN]] Defects in FLNA are the cause of periventricular nodular heterotopia type 1 (PVNH1) [MIM:[http://omim.org/entry/300049 300049]]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH is a developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.<ref>PMID:16299064</ref> <ref>PMID:11532987</ref> <ref>PMID:12410386</ref> <ref>PMID:11914408</ref> <ref>PMID:15249610</ref> Defects in FLNA are the cause of periventricular nodular heterotopia type 4 (PVNH4) [MIM:[http://omim.org/entry/300537 300537]]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood. Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:[http://omim.org/entry/311300 311300]]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.<ref>PMID:12612583</ref> <ref>PMID:15940695</ref> Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:[http://omim.org/entry/304120 304120]]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:[http://omim.org/entry/305620 305620]]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.<ref>PMID:12612583</ref> <ref>PMID:16596676</ref> Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:[http://omim.org/entry/309350 309350]]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.<ref>PMID:12612583</ref> Defects in FLNA are the cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:[http://omim.org/entry/300048 300048]]. CIIPX is characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.<ref>PMID:17357080</ref> Defects in FLNA are the cause of FG syndrome type 2 (FGS2) [MIM:[http://omim.org/entry/300321 300321]]. FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.<ref>PMID:17632775</ref> Defects in FLNA are the cause of terminal osseous dysplasia (TOD) [MIM:[http://omim.org/entry/300244 300244]]. A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.<ref>PMID:20598277</ref> Defects in FLNA are the cause of cardiac valvular dysplasia X-linked (CVDX) [MIM:[http://omim.org/entry/314400 314400]]. A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.<ref>PMID:17190868</ref> Note=Defects in FLNA may be a cause of macrothrombocytopenia, a disorder characterized by subnormal levels of blood platelets. Blood platelets are abonormally enlarged.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FLNA_HUMAN FLNA_HUMAN]] Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis.<ref>PMID:22121117</ref> [[http://www.uniprot.org/uniprot/FBLI1_HUMAN FBLI1_HUMAN]] Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion.<ref>PMID:12679033</ref> <ref>PMID:12496242</ref> <ref>PMID:18829455</ref> <ref>PMID:19074766</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Pentikainen, U]]
	[[Category: Seppala, J]]		[[Category: Seppala, J]]
	[[Category: Ylanne, J]]		[[Category: Ylanne, J]]
-	[[Category: ~~Pentikainen, U~~]]	+	[[Category: Actin binding protein]]
		+	[[Category: Adhesion]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Cytoskeleton]]
		+	[[Category: Immunoglobulin-like]]

OCA at 08:09, 22 April 2015

OCA — Wed, 22 Apr 2015 08:09:23 GMT

←Older revision		Revision as of 08:09, 22 April 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p3w is ON HOLD	+	The entry 4p3w is ON HOLD until Paper Publication

	Authors: Seppala, J., Pentikainen, U., Ylanne, J.		Authors: Seppala, J., Pentikainen, U., Ylanne, J.

OCA at 08:38, 18 February 2015

OCA — Wed, 18 Feb 2015 08:38:16 GMT

←Older revision		Revision as of 08:38, 18 February 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p3w is ON HOLD ~~until Paper Publication~~	+	The entry 4p3w is ON HOLD

	Authors: Seppala, J., Pentikainen, U., Ylanne, J.		Authors: Seppala, J., Pentikainen, U., Ylanne, J.

OCA at 14:45, 24 December 2014

OCA — Wed, 24 Dec 2014 14:45:33 GMT

←Older revision		Revision as of 14:45, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide		Description: Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide
		+	[[Category: Unreleased Structures]]
		+	[[Category: Seppala, J]]
		+	[[Category: Ylanne, J]]
		+	[[Category: Pentikainen, U]]

OCA at 05:44, 25 June 2014

OCA — Wed, 25 Jun 2014 05:44:45 GMT

←Older revision		Revision as of 05:44, 25 June 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p3w is ON HOLD	+	The entry 4p3w is ON HOLD until Paper Publication

	Authors: Seppala, J., Pentikainen, U., Ylanne, J.		Authors: Seppala, J., Pentikainen, U., Ylanne, J.

	Description: Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide		Description: Crystal structure of the human filamin A Ig-like domains 20-21 in complex with migfilin peptide

OCA: Protected "4p3w" [edit=sysop:move=sysop]

OCA — Wed, 19 Mar 2014 07:33:20 GMT

Protected "4p3w" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:33, 19 March 2014