6ou2: Difference between revisions

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'''Unreleased structure'''


The entry 6ou2 is ON HOLD
==Crystal Structure of the D478N Variant of the Myocilin Olfactomedin Domain==
 
<StructureSection load='6ou2' size='340' side='right'caption='[[6ou2]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ou2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OU2 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
[[Category: Unreleased Structures]]
<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=6ou2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ou2 OCA], [http://pdbe.org/6ou2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ou2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ou2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ou2 ProSAT]</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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hill, S E]]
[[Category: Kwon, M S]]
[[Category: Lieberman, R L]]
[[Category: Olfactomedin myocilin beta propeller]]
[[Category: Protein binding]]

Revision as of 08:59, 3 July 2019

Crystal Structure of the D478N Variant of the Myocilin Olfactomedin DomainCrystal Structure of the D478N Variant of the Myocilin Olfactomedin Domain

Structural highlights

6ou2 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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).[1]

Function

[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.[2] [3] [4] [5] [6] [7] [8] [9]

References

  1. ↑ Kaur K, Reddy AB, Mukhopadhyay A, Mandal AK, Hasnain SE, Ray K, Thomas R, Balasubramanian D, Chakrabarti S. Myocilin gene implicated in primary congenital glaucoma. Clin Genet. 2005 Apr;67(4):335-40. PMID:15733270 doi:http://dx.doi.org/10.1111/j.1399-0004.2005.00411.x
  2. ↑ Sakai H, Shen X, Koga T, Park BC, Noskina Y, Tibudan M, Yue BY. Mitochondrial association of myocilin, product of a glaucoma gene, in human trabecular meshwork cells. J Cell Physiol. 2007 Dec;213(3):775-84. PMID:17516541 doi:http://dx.doi.org/10.1002/jcp.21147
  3. ↑ Shen X, Koga T, Park BC, SundarRaj N, Yue BY. Rho GTPase and cAMP/protein kinase A signaling mediates myocilin-induced alterations in cultured human trabecular meshwork cells. J Biol Chem. 2008 Jan 4;283(1):603-12. Epub 2007 Nov 5. PMID:17984096 doi:http://dx.doi.org/10.1074/jbc.M708250200
  4. ↑ Goldwich A, Scholz M, Tamm ER. Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells. Histochem Cell Biol. 2009 Feb;131(2):167-80. doi: 10.1007/s00418-008-0518-4. Epub, 2008 Oct 15. PMID:18855004 doi:http://dx.doi.org/10.1007/s00418-008-0518-4
  5. ↑ Kwon HS, Lee HS, Ji Y, Rubin JS, Tomarev SI. Myocilin is a modulator of Wnt signaling. Mol Cell Biol. 2009 Apr;29(8):2139-54. doi: 10.1128/MCB.01274-08. Epub 2009 Feb, 2. PMID:19188438 doi:http://dx.doi.org/10.1128/MCB.01274-08
  6. ↑ Koga T, Shen X, Park JS, Qiu Y, Park BC, Shyam R, Yue BY. Differential effects of myocilin and optineurin, two glaucoma genes, on neurite outgrowth. Am J Pathol. 2010 Jan;176(1):343-52. doi: 10.2353/ajpath.2010.090194. Epub 2009, Dec 3. PMID:19959812 doi:http://dx.doi.org/10.2353/ajpath.2010.090194
  7. ↑ Kwon HS, Tomarev SI. Myocilin, a glaucoma-associated protein, promotes cell migration through activation of integrin-focal adhesion kinase-serine/threonine kinase signaling pathway. J Cell Physiol. 2011 Dec;226(12):3392-402. doi: 10.1002/jcp.22701. PMID:21656515 doi:http://dx.doi.org/10.1002/jcp.22701
  8. ↑ Kwon HS, Johnson TV, Tomarev SI. Myocilin stimulates osteogenic differentiation of mesenchymal stem cells through mitogen-activated protein kinase signaling. J Biol Chem. 2013 Jun 7;288(23):16882-94. doi: 10.1074/jbc.M112.422972. Epub 2013, Apr 29. PMID:23629661 doi:http://dx.doi.org/10.1074/jbc.M112.422972
  9. ↑ Kwon HS, Johnson TV, Joe MK, Abu-Asab M, Zhang J, Chan CC, Tomarev SI. Myocilin mediates myelination in the peripheral nervous system through ErbB2/3 signaling. J Biol Chem. 2013 Sep 13;288(37):26357-71. doi: 10.1074/jbc.M112.446138. Epub, 2013 Jul 29. PMID:23897819 doi:http://dx.doi.org/10.1074/jbc.M112.446138

6ou2, resolution 1.96Å

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