3sov - Revision history

OCA at 06:10, 17 October 2024

2024-10-17T06:10:48Z

← Older revision		Revision as of 06:10, 17 October 2024
Line 3:		Line 3:
	<StructureSection load='3sov' size='340' side='right'caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>		<StructureSection load='3sov' size='340' side='right'caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOV FirstGlance]. <br>		<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOV FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FUC:ALPHA-L~~-~~FUCOSE'>FUC</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.27Å</td></tr>
	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=~~NH2~~:~~AMINO+GROUP~~'>~~NH2~~</scene><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[3sob\|3sob]], [[3soq\|3soq]]~~</~~div~~><~~/td></tr>~~
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">LRP6 ([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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [https://pdbe.org/3sov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [https://www.ebi.ac.uk/pdbsum/3sov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sov 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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [https://pdbe.org/3sov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [https://www.ebi.ac.uk/pdbsum/3sov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sov ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[https://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[https://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[https://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[https://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>		[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> ~~[[https://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>~~		[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Bourhis, E]]		[[Category: Bourhis E]]
	[[Category: Cochran~~, A G~~]]		[[Category: Cochran AG]]
	[[Category: Franke, Y]]		[[Category: Franke Y]]
	[[Category: Rouge, L]]		[[Category: Rouge L]]
	[[Category: Wang, W]]		[[Category: Wang W]]
	[[Category: Wu, Y]]		[[Category: Wu Y]]
	[[Category: Zhang, Y]]		[[Category: Zhang Y]]
	~~[[Category: Beta propeller]]~~
	~~[[Category: Protein binding-antagonist complex~~]]

OCA at 08:04, 29 June 2022

2022-06-29T08:04:31Z

← Older revision		Revision as of 08:04, 29 June 2022
Line 1:		Line 1:

	==The structure of a beta propeller domain in complex with peptide S==		==The structure of a beta propeller domain in complex with peptide S==
	<StructureSection load='3sov' size='340' side='right' caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>		<StructureSection load='3sov' size='340' side='right'caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3SOV FirstGlance]. <br>		<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3sob\|3sob]], [[3soq\|3soq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sob\|3sob]], [[3soq\|3soq]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LRP6 ([~~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">LRP6 ([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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [~~http~~://pdbe.org/3sov PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3sov PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3sov 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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [https://pdbe.org/3sov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [https://www.ebi.ac.uk/pdbsum/3sov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sov ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[~~http~~://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[~~http~~://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[~~http~~://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[~~http~~://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>		[[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[https://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[https://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[https://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[https://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> [[~~http~~://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>		[[https://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> [[https://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Bourhis, E]]		[[Category: Bourhis, E]]
	[[Category: Cochran, A G]]		[[Category: Cochran, A G]]

OCA at 20:38, 5 August 2016

2016-08-05T20:38:25Z

← Older revision		Revision as of 20:38, 5 August 2016
Line 1:		Line 1:

	==The structure of a beta propeller domain in complex with peptide S==		==The structure of a beta propeller domain in complex with peptide S==
	<StructureSection load='3sov' size='340' side='right' caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>		<StructureSection load='3sov' size='340' side='right' caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOV FirstGlance]. <br>		<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3sob\|3sob]], [[3soq\|3soq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3sob\|3sob]], [[3soq\|3soq]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LRP6 ([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">LRP6 ([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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [http://www.ebi.ac.uk/pdbsum/3sov 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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [http://pdbe.org/3sov PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [http://www.ebi.ac.uk/pdbsum/3sov PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sov ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	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 3sov" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Bourhis, E]]		[[Category: Bourhis, E]]
	[[Category: Cochran, A G]]		[[Category: Cochran, A G]]

OCA at 07:20, 21 December 2014

2014-12-21T07:20:19Z

← Older revision		Revision as of 07:20, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3sov\| PDB=3sov \| SCENE= }}~~		==The structure of a beta propeller domain in complex with peptide S==
	===The structure of a beta propeller domain in complex with peptide S===		<StructureSection load='3sov' size='340' side='right' caption='[[3sov]], [[Resolution\|resolution]] 1.27Å' scene=''>
	~~{{ABSTRACT_PUBMED_21944579}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3sov]] is a 2 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=3SOV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOV FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3sob\|3sob]], [[3soq\|3soq]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LRP6 ([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=3sov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sov OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sov RCSB], [http://www.ebi.ac.uk/pdbsum/3sov PDBsum]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[http://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[http://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[http://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>		[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[http://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[http://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[http://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>
			== Function ==
	==Function==
	[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>		[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The Wnt pathway inhibitors DKK1 and sclerostin (SOST) are important therapeutic targets in diseases involving bone loss or damage. It has been appreciated that Wnt coreceptors LRP5/6 are also important, as human missense mutations that result in bone overgrowth (bone mineral density, or BMD, mutations) cluster to the E1 propeller domain of LRP5. Here, we report a crystal structure of LRP6 E1 bound to an antibody, revealing that the E1 domain is a peptide recognition module. Remarkably, the consensus E1 binding sequence is a close match to a conserved tripeptide motif present in all Wnt inhibitors that bind LRP5/6. We show that this motif is important for DKK1 and SOST binding to LRP6 and for inhibitory function, providing a detailed structural explanation for the effect of the BMD mutations.

	~~==About this Structure==~~		Wnt antagonists bind through a short peptide to the first beta-propeller domain of LRP5/6.,Bourhis E, Wang W, Tam C, Hwang J, Zhang Y, Spittler D, Huang OW, Gong Y, Estevez A, Zilberleyb I, Rouge L, Chiu C, Wu Y, Costa M, Hannoush RN, Franke Y, Cochran AG Structure. 2011 Oct 12;19(10):1433-42. Epub 2011 Sep 22. PMID:21944579<ref>PMID:21944579</ref>
	~~[[3sov]] is~~ a ~~2 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=3SOV OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:021944579</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bourhis, E.]]		[[Category: Bourhis, E]]
	[[Category: Cochran, A G.]]		[[Category: Cochran, A G]]
	[[Category: Franke, Y.]]		[[Category: Franke, Y]]
	[[Category: Rouge, L.]]		[[Category: Rouge, L]]
	[[Category: Wang, W.]]		[[Category: Wang, W]]
	[[Category: Wu, Y.]]		[[Category: Wu, Y]]
	[[Category: Zhang, Y.]]		[[Category: Zhang, Y]]
	[[Category: Beta propeller]]		[[Category: Beta propeller]]
	[[Category: Protein binding-antagonist complex]]		[[Category: Protein binding-antagonist complex]]

OCA at 05:26, 28 August 2013

2013-08-28T05:26:25Z

← Older revision		Revision as of 05:26, 28 August 2013
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	~~[[Image:3sov.jpg\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3sov", 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_3sov\| PDB=3sov \| SCENE= }}		{{STRUCTURE_3sov\| PDB=3sov \| SCENE= }}
			===The structure of a beta propeller domain in complex with peptide S===
			{{ABSTRACT_PUBMED_21944579}}

	===The ~~structure~~ of a ~~beta propeller domain~~ in ~~complex with peptide S=~~==		==Disease==
			[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Coronary artery disease - hyperlipidemia - hypertension - diabetes - osteoporosis. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Defects in SOST are the cause of sclerosteosis type 1 (SOST1) [MIM:[http://omim.org/entry/269500 269500]]. An autosomal recessive sclerosing bone dysplasia characterized by a generalized hyperostosis and sclerosis leading to a markedly thickened skull, with mandible, ribs, clavicles and all long bones also being affected. Due to narrowing of the foramina of the cranial nerves, facial nerve palsy, hearing loss and atrophy of the optic nerves can occur. Sclerosteosis is clinically and radiologically very similar to van Buchem disease, mainly differentiated by hand malformations and a large stature in sclerosteosis patients.<ref>PMID:11181578</ref> <ref>PMID:11179006</ref> <ref>PMID:20583295</ref> Defects in SOST are a cause of van Buchem disease (VBCH) [MIM:[http://omim.org/entry/239100 239100]]. An autosomal recessive sclerosing bone dysplasia characterized by endosteal hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of the long bones. Affected patients present a symmetrically increased thickness of bones, most frequently found as an enlarged jawbone, but also an enlargement of the skull, ribs, diaphysis of long bones, as well as tubular bones of hands and feet. The clinical consequence of increased thickness of the skull include facial nerve palsy causing hearing loss, visual problems, neurological pain, and, very rarely, blindness as a consequence of optic atrophy. Serum alkaline phosphatase levels are elevated. Note=A 52 kb deletion downstream of SOST results in SOST transcription suppression causing van Buchem disease.<ref>PMID:11836356</ref> Defects in SOST are a cause of craniodiaphyseal dysplasia autosomal dominant (CDD) [MIM:[http://omim.org/entry/122860 122860]]. A severe bone dysplasia characterized by massive generalized hyperostosis and sclerosis, especially involving the skull and facial bones. The sclerosis is so severe that the resulting facial distortion is referred to as 'leontiasis ossea' (leonine faces) and the bone deposition results in progressive stenosis of craniofacial foramina. Respiratory obstruction due to choanal stenosis compromises the clinical outcomes of affected patients. Note=Heterozygous mutations located in the secretion signal of the SOST gene prevent sclerostin secretion and can be responsible for craniodiaphyseal dysplasia.<ref>PMID:21221996</ref>

			==Function==
			[[http://www.uniprot.org/uniprot/LRP6_HUMAN LRP6_HUMAN]] Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity).<ref>PMID:11448771</ref> <ref>PMID:11357136</ref> <ref>PMID:15778503</ref> <ref>PMID:16341017</ref> <ref>PMID:16513652</ref> <ref>PMID:17400545</ref> <ref>PMID:17326769</ref> <ref>PMID:19107203</ref> <ref>PMID:19801552</ref> <ref>PMID:19293931</ref> [[http://www.uniprot.org/uniprot/SOST_HUMAN SOST_HUMAN]] Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.<ref>PMID:15908424</ref>

	==About this Structure==		==About this Structure==
	[[3sov]] is a 2 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=3SOV OCA].		[[3sov]] is a 2 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=3SOV OCA].

			==Reference==
			<ref group="xtra">PMID:021944579</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bourhis, E.]]		[[Category: Bourhis, E.]]

OCA at 06:13, 21 September 2011

2011-09-21T06:13:18Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3sov.jpg|left|200px]]
-The entry 3sov is ON HOLD  until Paper Publication
+<!--
-Authors: Wang, W., Bourhis, E., Zhang, Y., Rouge, L., Wu, Y., Franke, Y., Cochran, A.G.
+===The structure of a beta propeller domain in complex with peptide S===
-Description: The structure of a beta propeller domain in complex with peptide S

OCA at 05:48, 17 August 2011

2011-08-17T05:48:59Z

← Older revision		Revision as of 05:48, 17 August 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3sov is ON HOLD		The entry 3sov is ON HOLD until Paper Publication

	Authors: Wang, W., Bourhis, E., Zhang, Y., Rouge, L., Wu, Y., Franke, Y., Cochran, A.G.		Authors: Wang, W., Bourhis, E., Zhang, Y., Rouge, L., Wu, Y., Franke, Y., Cochran, A.G.

	Description: The structure of a beta propeller domain in complex with peptide S		Description: The structure of a beta propeller domain in complex with peptide S

OCA at 05:40, 27 July 2011

2011-07-27T05:40:33Z

← Older revision		Revision as of 05:40, 27 July 2011
Line 3:		Line 3:
	The entry 3sov is ON HOLD		The entry 3sov is ON HOLD

	Authors: Wang, W., Bourhis, E., Zhang, Y, Rouge, L, Wu, Y, Franke, Y, Cochran, A. G.		Authors: Wang, W., Bourhis, E., Zhang, Y., Rouge, L., Wu, Y., Franke, Y., Cochran, A.G.

	Description: The structure of a beta propeller domain in complex with peptide S		Description: The structure of a beta propeller domain in complex with peptide S

OCA: Protected "3sov" [edit=sysop:move=sysop]

2011-07-06T18:31:21Z

Protected "3sov" [edit=sysop:move=sysop]

← Older revision	Revision as of 18:31, 6 July 2011
(No difference)

OCA: New page: '''Unreleased structure''' The entry 3sov is ON HOLD Authors: Wang, W., Bourhis, E., Zhang, Y, Rouge, L, Wu, Y, Franke, Y, Cochran, A. G. Description: The structure of a beta propeller...

2011-07-06T18:31:20Z

New page: '''Unreleased structure''' The entry 3sov is ON HOLD Authors: Wang, W., Bourhis, E., Zhang, Y, Rouge, L, Wu, Y, Franke, Y, Cochran, A. G. Description: The structure of a beta propeller...

New page

'''Unreleased structure'''

The entry 3sov is ON HOLD

Authors: Wang, W., Bourhis, E., Zhang, Y, Rouge, L, Wu, Y, Franke, Y, Cochran, A. G.

Description: The structure of a beta propeller domain in complex with peptide S