4wxq - Revision history

OCA at 21:02, 12 April 2023

OCA — Wed, 12 Apr 2023 21:02:47 GMT

←Older revision		Revision as of 21:02, 12 April 2023
Line 3:		Line 3:
	<StructureSection load='4wxq' size='340' side='right'caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4wxq' size='340' side='right'caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxq]] 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=4WXQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxq]] 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=4WXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [https://pdbe.org/4wxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [https://www.ebi.ac.uk/pdbsum/4wxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxq ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MYOC, GLC1A, TIGR ([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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [~~http~~://pdbe.org/4wxq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wxq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN]] Congenital glaucoma;Juvenile glaucoma. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270).<ref>PMID:15733270</ref>	+	[https://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN] Congenital glaucoma;Juvenile glaucoma. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270).<ref>PMID:15733270</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN]] Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork.<ref>PMID:17516541</ref> <ref>PMID:17984096</ref> <ref>PMID:18855004</ref> <ref>PMID:19188438</ref> <ref>PMID:19959812</ref> <ref>PMID:21656515</ref> <ref>PMID:23629661</ref> <ref>PMID:23897819</ref>	+	[https://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN] Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork.<ref>PMID:17516541</ref> <ref>PMID:17984096</ref> <ref>PMID:18855004</ref> <ref>PMID:19188438</ref> <ref>PMID:19959812</ref> <ref>PMID:21656515</ref> <ref>PMID:23629661</ref> <ref>PMID:23897819</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: Donegan~~, R K~~]]	+	[[Category: Donegan RK]]
-	[[Category: Lieberman~~, R L~~]]	+	[[Category: Lieberman RL]]
-	[[Category: Orwig~~, S D~~]]	+	[[Category: Orwig SD]]
-	[[Category: Turnage~~, K C]]~~	+	[[Category: Turnage KC]]
-	~~[[Category: Bladed propeller]]~~	+
-	~~[[Category: Beta propeller]]~~	+
-	~~[[Category: Olfactomedin]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 08:31, 23 May 2019

OCA — Thu, 23 May 2019 08:31:38 GMT

←Older revision		Revision as of 08:31, 23 May 2019
Line 1:		Line 1:

	==Crystal Structure of the Myocilin Olfactomedin Domain==		==Crystal Structure of the Myocilin Olfactomedin Domain==
-	<StructureSection load='4wxq' size='340' side='right' caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='4wxq' size='340' side='right'caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxq]] 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=4WXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MYOC, GLC1A, TIGR ([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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [http://pdbe.org/4wxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [http://www.ebi.ac.uk/pdbsum/4wxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxq 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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [http://pdbe.org/4wxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [http://www.ebi.ac.uk/pdbsum/4wxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxq ProSAT]</span></td></tr>
	</table>		</table>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Donegan, R K]]		[[Category: Donegan, R K]]
	[[Category: Lieberman, R L]]		[[Category: Lieberman, R L]]

OCA at 00:25, 26 January 2017

OCA — Thu, 26 Jan 2017 00:25:45 GMT

←Older revision		Revision as of 00:25, 26 January 2017
Line 1:		Line 1:
		+
	==Crystal Structure of the Myocilin Olfactomedin Domain==		==Crystal Structure of the Myocilin Olfactomedin Domain==
	<StructureSection load='4wxq' size='340' side='right' caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='4wxq' size='340' side='right' caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [http://www.ebi.ac.uk/pdbsum/4wxq 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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [http://pdbe.org/4wxq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [http://www.ebi.ac.uk/pdbsum/4wxq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4wxq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:15, 1 April 2015

OCA — Wed, 01 Apr 2015 13:15:34 GMT

←Older revision		Revision as of 13:15, 1 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal Structure of the Myocilin Olfactomedin Domain==
		+	<StructureSection load='4wxq' size='340' side='right' caption='[[4wxq]], [[Resolution\|resolution]] 2.15Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4wxq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wxs\|4wxs]], [[4wxu\|4wxu]]</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=4wxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxq RCSB], [http://www.ebi.ac.uk/pdbsum/4wxq PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN]] Congenital glaucoma;Juvenile glaucoma. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270).<ref>PMID:15733270</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MYOC_HUMAN MYOC_HUMAN]] Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork.<ref>PMID:17516541</ref> <ref>PMID:17984096</ref> <ref>PMID:18855004</ref> <ref>PMID:19188438</ref> <ref>PMID:19959812</ref> <ref>PMID:21656515</ref> <ref>PMID:23629661</ref> <ref>PMID:23897819</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Olfactomedin (OLF) domain-containing proteins play roles in fundamental cellular processes and have been implicated in disorders ranging from glaucoma, cancers and inflammatory bowel disorder, to attention deficit disorder and childhood obesity. We solved crystal structures of the OLF domain of myocilin (myoc-OLF), the best studied such domain to date. Mutations in myoc-OLF are causative in the autosomal dominant inherited form of the prevalent ocular disorder glaucoma. The structures reveal a new addition to the small family of five-bladed beta-propellers. Propellers are most well known for their ability to act as hubs for protein-protein interactions, a function that seems most likely for myoc-OLF, but they can also act as enzymes. A calcium ion, sodium ion and glycerol molecule were identified within a central hydrophilic cavity that is accessible via movements of surface loop residues. By mapping familial glaucoma-associated lesions onto the myoc-OLF structure, three regions sensitive to aggregation have been identified, with direct applicability to differentiating between neutral and disease-causing non-synonymous mutations documented in the human population worldwide. Evolutionary analysis mapped onto the myoc-OLF structure reveals conserved and divergent regions for possible overlapping and distinctive functional protein-protein or protein-ligand interactions across the broader OLF domain family. While deciphering the specific normal biological functions, ligands and binding partners for OLF domains will likely continue to be a challenging long-term experimental pursuit, atomic detail structural knowledge of myoc-OLF is a valuable guide for understanding the implications of glaucoma-associated mutations and will help focus future studies of this biomedically important domain family.

-	~~The entry 4wxq is ON HOLD until Nov 14 2016~~	+	Structural basis for misfolding in myocilin-associated glaucoma.,Donegan RK, Hill SE, Freeman DM, Nguyen E, Orwig SD, Turnage KC, Lieberman RL Hum Mol Genet. 2015 Apr 15;24(8):2111-24. doi: 10.1093/hmg/ddu730. Epub 2014 Dec , 18. PMID:25524706<ref>PMID:25524706</ref>

-	~~Authors: Orwig~~, S.D.~~, Turnage, K.C.,~~ Donegan, R.K., Lieberman, R.L.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal Structure of the Myocilin Olfactomedin Domain~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: ~~Donegan~~, R.K]]	+	__TOC__
-	[[Category: ~~Orwig, S.D~~]]	+	</StructureSection>
-	[[Category: ~~Lieberman, R.L~~]]	+	[[Category: Donegan, R K]]
-	[[Category: ~~Turnage, K.C~~]]	+	[[Category: Lieberman, R L]]
		+	[[Category: Orwig, S D]]
		+	[[Category: Turnage, K C]]
		+	[[Category: Bladed propeller]]
		+	[[Category: Beta propeller]]
		+	[[Category: Olfactomedin]]
		+	[[Category: Protein binding]]

OCA at 20:10, 24 December 2014

OCA — Wed, 24 Dec 2014 20:10:38 GMT

←Older revision		Revision as of 20:10, 24 December 2014
Line 6:		Line 6:

	Description: Crystal Structure of the Myocilin Olfactomedin Domain		Description: Crystal Structure of the Myocilin Olfactomedin Domain
		+	[[Category: Unreleased Structures]]
		+	[[Category: Donegan, R.K]]
		+	[[Category: Orwig, S.D]]
		+	[[Category: Lieberman, R.L]]
		+	[[Category: Turnage, K.C]]

OCA at 08:41, 3 December 2014

OCA — Wed, 03 Dec 2014 08:41:33 GMT

←Older revision		Revision as of 08:41, 3 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4wxq is ON HOLD	+	The entry 4wxq is ON HOLD until Nov 14 2016

	Authors: Orwig, S.D., Turnage, K.C., Donegan, R.K., Lieberman, R.L.		Authors: Orwig, S.D., Turnage, K.C., Donegan, R.K., Lieberman, R.L.

	Description: Crystal Structure of the Myocilin Olfactomedin Domain		Description: Crystal Structure of the Myocilin Olfactomedin Domain

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

OCA — Wed, 26 Nov 2014 07:11:53 GMT

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

←Older revision

Revision as of 07:11, 26 November 2014

OCA: New page: '''Unreleased structure''' The entry 4wxq is ON HOLD Authors: Orwig, S.D., Turnage, K.C., Donegan, R.K., Lieberman, R.L. Description: Crystal Structure of the Myocilin Olfactomedin Dom...

OCA — Wed, 26 Nov 2014 07:11:52 GMT

New page: '''Unreleased structure''' The entry 4wxq is ON HOLD Authors: Orwig, S.D., Turnage, K.C., Donegan, R.K., Lieberman, R.L. Description: Crystal Structure of the Myocilin Olfactomedin Dom...

New page

'''Unreleased structure'''

The entry 4wxq is ON HOLD

Authors: Orwig, S.D., Turnage, K.C., Donegan, R.K., Lieberman, R.L.

Description: Crystal Structure of the Myocilin Olfactomedin Domain