3s67 - Revision history

OCA at 12:48, 14 March 2024

OCA — Thu, 14 Mar 2024 12:48:02 GMT

←Older revision		Revision as of 12:48, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3s67' size='340' side='right'caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>		<StructureSection load='3s67' size='340' side='right'caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S67 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s67]] is a 1 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=3S67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S67 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.26Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([https://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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [https://pdbe.org/3s67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [https://www.ebi.ac.uk/pdbsum/3s67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s67 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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [https://pdbe.org/3s67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [https://www.ebi.ac.uk/pdbsum/3s67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s67 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[https://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[https://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>	+	[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[https://omim.org/entry/105150 105150]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[https://omim.org/entry/611953 611953]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.	+	[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Wild-type human cystatin C (hCC wt) is a low-molecular-mass protein (120 amino-acid residues, 13 343 Da) that is found in all nucleated cells. Physiologically, it functions as a potent regulator of cysteine protease activity. While the biologically active hCC wt is a monomeric protein, all crystallization efforts to date have resulted in a three-dimensional domain-swapped dimeric structure. In the recently published structure of a mutated hCC, the monomeric fold was preserved by a stabilization of the conformationally constrained loop L1 caused by a single amino-acid substitution: Val57Asn. Additional hCC mutants were obtained in order to elucidate the relationship between the stability of the L1 loop and the propensity of human cystatin C to dimerize. In one mutant Val57 was substituted by an aspartic acid residue, which is favoured in beta-turns, and in the second mutant proline, a residue known for broadening turns, was substituted for the same Val57. Here, 2.26 and 3.0 A resolution crystal structures of the V57D andV57P mutants of hCC are reported and their dimeric architecture is discussed in terms of the stabilization and destabilization effects of the introduced mutations.	+
-		+
-	Structural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic protein.,Orlikowska M, Szymanska A, Borek D, Otwinowski Z, Skowron P, Jankowska E Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):577-86. doi:, 10.1107/S0907444912051657. Epub 2013 Mar 14. PMID:23519666<ref>PMID:23519666</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3s67" style="background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Borek, D]]	+	[[Category: Borek D]]
-	[[Category: Jankowska, E]]	+	[[Category: Jankowska E]]
-	[[Category: Orlikowska, M]]	+	[[Category: Orlikowska M]]
-	[[Category: Otwinowski, Z]]	+	[[Category: Otwinowski Z]]
-	[[Category: Skowron, P]]	+	[[Category: Skowron P]]
-	[[Category: Szymanska, A]]	+	[[Category: Szymanska A]]
-	~~[[Category: Hydrolase inhibitor~~]]	+

OCA at 10:39, 22 June 2022

OCA — Wed, 22 Jun 2022 10:39:55 GMT

←Older revision		Revision as of 10:39, 22 June 2022
Line 1:		Line 1:

	==Crystal structure of V57P mutant of human cystatin C==		==Crystal structure of V57P mutant of human cystatin C==
-	<StructureSection load='3s67' size='340' side='right' caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>	+	<StructureSection load='3s67' size='340' side='right'caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s67]] is a 1 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=3S67 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3S67 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S67 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([https://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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [~~http~~://pdbe.org/3s67 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3s67 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3s67 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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [https://pdbe.org/3s67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [https://www.ebi.ac.uk/pdbsum/3s67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s67 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[~~http~~://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[~~http~~://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>	+	[[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[https://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[https://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.	+	[[https://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Borek, D]]		[[Category: Borek, D]]
	[[Category: Jankowska, E]]		[[Category: Jankowska, E]]

OCA at 12:58, 5 August 2016

OCA — Fri, 05 Aug 2016 12:58:57 GMT

←Older revision		Revision as of 12:58, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of V57P mutant of human cystatin C==		==Crystal structure of V57P mutant of human cystatin C==
	<StructureSection load='3s67' size='340' side='right' caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>		<StructureSection load='3s67' size='340' side='right' caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3s67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S67 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3s67]] is a 1 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=3S67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S67 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [http://www.ebi.ac.uk/pdbsum/3s67 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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [http://pdbe.org/3s67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [http://www.ebi.ac.uk/pdbsum/3s67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s67 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 3s67" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Borek, D]]		[[Category: Borek, D]]
	[[Category: Jankowska, E]]		[[Category: Jankowska, E]]

OCA at 06:30, 21 December 2014

OCA — Sun, 21 Dec 2014 06:30:43 GMT

←Older revision		Revision as of 06:30, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}~~	+	==Crystal structure of V57P mutant of human cystatin C==
-	===Crystal structure of V57P mutant of human cystatin C===	+	<StructureSection load='3s67' size='340' side='right' caption='[[3s67]], [[Resolution\|resolution]] 2.26Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23519666}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3s67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S67 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g96\|1g96]], [[1r4c\|1r4c]], [[1tij\|1tij]], [[3gax\|3gax]], [[3nx0\|3nx0]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CST3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3s67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s67 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s67 RCSB], [http://www.ebi.ac.uk/pdbsum/3s67 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[http://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[http://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>		[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[http://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[http://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.		[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Wild-type human cystatin C (hCC wt) is a low-molecular-mass protein (120 amino-acid residues, 13 343 Da) that is found in all nucleated cells. Physiologically, it functions as a potent regulator of cysteine protease activity. While the biologically active hCC wt is a monomeric protein, all crystallization efforts to date have resulted in a three-dimensional domain-swapped dimeric structure. In the recently published structure of a mutated hCC, the monomeric fold was preserved by a stabilization of the conformationally constrained loop L1 caused by a single amino-acid substitution: Val57Asn. Additional hCC mutants were obtained in order to elucidate the relationship between the stability of the L1 loop and the propensity of human cystatin C to dimerize. In one mutant Val57 was substituted by an aspartic acid residue, which is favoured in beta-turns, and in the second mutant proline, a residue known for broadening turns, was substituted for the same Val57. Here, 2.26 and 3.0 A resolution crystal structures of the V57D andV57P mutants of hCC are reported and their dimeric architecture is discussed in terms of the stabilization and destabilization effects of the introduced mutations.

-	~~==About this Structure==~~	+	Structural characterization of V57D and V57P mutants of human cystatin C, an amyloidogenic protein.,Orlikowska M, Szymanska A, Borek D, Otwinowski Z, Skowron P, Jankowska E Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):577-86. doi:, 10.1107/S0907444912051657. Epub 2013 Mar 14. PMID:23519666<ref>PMID:23519666</ref>
-	~~[[3s67]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=3S67 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Borek, D.]]	+	[[Category: Borek, D]]
-	[[Category: Jankowska, E.]]	+	[[Category: Jankowska, E]]
-	[[Category: Orlikowska, M.]]	+	[[Category: Orlikowska, M]]
-	[[Category: Otwinowski, Z.]]	+	[[Category: Otwinowski, Z]]
-	[[Category: Skowron, P.]]	+	[[Category: Skowron, P]]
-	[[Category: Szymanska, A.]]	+	[[Category: Szymanska, A]]
	[[Category: Hydrolase inhibitor]]		[[Category: Hydrolase inhibitor]]

OCA at 22:32, 3 April 2013

OCA — Wed, 03 Apr 2013 22:32:42 GMT

←Older revision		Revision as of 22:32, 3 April 2013
Line 1:		Line 1:
	{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}		{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}
	===Crystal structure of V57P mutant of human cystatin C===		===Crystal structure of V57P mutant of human cystatin C===
		+	{{ABSTRACT_PUBMED_23519666}}

	==Disease==		==Disease==
-	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[http://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref><ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[http://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>	+	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[http://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref> <ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[http://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>

	==Function==		==Function==

OCA at 22:43, 24 March 2013

OCA — Sun, 24 Mar 2013 22:43:20 GMT

←Older revision		Revision as of 22:43, 24 March 2013
Line 1:		Line 1:
-	[[Image:3s67.png\|left\|200px]]
-
	{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}		{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}
-
	===Crystal structure of V57P mutant of human cystatin C===		===Crystal structure of V57P mutant of human cystatin C===

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] Defects in CST3 are the cause of amyloidosis type 6 (AMYL6) [MIM:[http://omim.org/entry/105150 105150]]; also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.<ref>PMID:2541223</ref><ref>PMID:1352269</ref> Genetic variations in CST3 are associated with age-related macular degeneration type 11 (ARMD11) [MIM:[http://omim.org/entry/611953 611953]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:11815350</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CYTC_HUMAN CYTC_HUMAN]] As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.

	==About this Structure==		==About this Structure==
	[[3s67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA].		[[3s67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Borek, D.]]		[[Category: Borek, D.]]

OCA at 12:53, 27 February 2013

OCA — Wed, 27 Feb 2013 12:53:25 GMT

←Older revision		Revision as of 12:53, 27 February 2013
Line 1:		Line 1:
-	[[Image:3s67.~~jpg~~\|left\|200px]]	+	[[Image:3s67.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3s67", 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_3s67\| PDB=3s67 \| SCENE= }}		{{STRUCTURE_3s67\| PDB=3s67 \| SCENE= }}

OCA at 05:59, 30 May 2012

OCA — Wed, 30 May 2012 05:59:27 GMT

←Older revision		Revision as of 05:59, 30 May 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3s67.jpg\|left\|200px]]

-	The ~~entry 3s67~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3s67", 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_3s67\| PDB=3s67 \| SCENE= }}

-	~~Authors: Orlikowska, M., Szymanska, A., Borek, D., Otwinowski, Z., Skowron, P., Jankowska, E.~~	+	===Crystal structure of V57P mutant of human cystatin C===

-	~~Description: Crystal~~ structure ~~of V57P mutant of human cystatin C~~	+
		+	==About this Structure==
		+	[[3s67]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S67 OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Borek, D.]]
		+	[[Category: Jankowska, E.]]
		+	[[Category: Orlikowska, M.]]
		+	[[Category: Otwinowski, Z.]]
		+	[[Category: Skowron, P.]]
		+	[[Category: Szymanska, A.]]
		+	[[Category: Hydrolase inhibitor]]

OCA at 05:41, 29 June 2011

OCA — Wed, 29 Jun 2011 05:41:57 GMT

←Older revision		Revision as of 05:41, 29 June 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3s67 is ON HOLD	+	The entry 3s67 is ON HOLD until Paper Publication

	Authors: Orlikowska, M., Szymanska, A., Borek, D., Otwinowski, Z., Skowron, P., Jankowska, E.		Authors: Orlikowska, M., Szymanska, A., Borek, D., Otwinowski, Z., Skowron, P., Jankowska, E.

	Description: Crystal structure of V57P mutant of human cystatin C		Description: Crystal structure of V57P mutant of human cystatin C

OCA at 04:53, 8 June 2011

OCA — Wed, 08 Jun 2011 04:53:28 GMT

←Older revision		Revision as of 04:53, 8 June 2011
Line 3:		Line 3:
	The entry 3s67 is ON HOLD		The entry 3s67 is ON HOLD

-	Authors: Orlikowska, M. , Szymanska, A., Borek, D., Otwinowski, Z., Skowron, P., Jankowska, E	+	Authors: Orlikowska, M., Szymanska, A., Borek, D., Otwinowski, Z., Skowron, P., Jankowska, E.

	Description: Crystal structure of V57P mutant of human cystatin C		Description: Crystal structure of V57P mutant of human cystatin C