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'''Unreleased structure'''


The entry 6ocf is ON HOLD  until Paper Publication
==The crystal structure of VASH1-SVBP complex==
 
<StructureSection load='6ocf' size='340' side='right'caption='[[6ocf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
Authors: Li, F., Luo, X., Yu, H.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ocf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OCF FirstGlance]. <br>
Description: The crystal structure of VASH1-SVBP complex
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
[[Category: Yu, H]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tubulinyl-Tyr_carboxypeptidase Tubulinyl-Tyr carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.17 3.4.17.17] </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=6ocf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ocf OCA], [http://pdbe.org/6ocf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ocf RCSB], [http://www.ebi.ac.uk/pdbsum/6ocf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ocf ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/VASH1_HUMAN VASH1_HUMAN]] Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146869). Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:15467828, PubMed:16488400, PubMed:16707096, PubMed:19204325). This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (PubMed:15467828, PubMed:16488400, PubMed:16707096).<ref>PMID:15467828</ref> <ref>PMID:16488400</ref> <ref>PMID:16707096</ref> <ref>PMID:19204325</ref> <ref>PMID:29146869</ref>  [[http://www.uniprot.org/uniprot/SVBP_HUMAN SVBP_HUMAN]] Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin (PubMed:29146869). Also required to enhance the solubility and secretion of VASH1 and VASH2 (PubMed:20736312, PubMed:27879017).<ref>PMID:20736312</ref> <ref>PMID:27879017</ref> <ref>PMID:29146869</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tubulinyl-Tyr carboxypeptidase]]
[[Category: Li, F]]
[[Category: Li, F]]
[[Category: Luo, X]]
[[Category: Luo, X]]
[[Category: Yu, H]]
[[Category: Hydrolase-protein binding complex]]
[[Category: Microtubule modification]]
[[Category: Tubulin carboxypeptidase]]
[[Category: Tubulin detyrosination]]
[[Category: Vash1-svbp complex]]

Revision as of 09:58, 26 June 2019

The crystal structure of VASH1-SVBP complexThe crystal structure of VASH1-SVBP complex

Structural highlights

6ocf is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Activity:Tubulinyl-Tyr carboxypeptidase, with EC number 3.4.17.17
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VASH1_HUMAN] Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146869). Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:15467828, PubMed:16488400, PubMed:16707096, PubMed:19204325). This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (PubMed:15467828, PubMed:16488400, PubMed:16707096).[1] [2] [3] [4] [5] [SVBP_HUMAN] Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin (PubMed:29146869). Also required to enhance the solubility and secretion of VASH1 and VASH2 (PubMed:20736312, PubMed:27879017).[6] [7] [8]

References

  1. ↑ Watanabe K, Hasegawa Y, Yamashita H, Shimizu K, Ding Y, Abe M, Ohta H, Imagawa K, Hojo K, Maki H, Sonoda H, Sato Y. Vasohibin as an endothelium-derived negative feedback regulator of angiogenesis. J Clin Invest. 2004 Oct;114(7):898-907. doi: 10.1172/JCI21152. PMID:15467828 doi:http://dx.doi.org/10.1172/JCI21152
  2. ↑ Sonoda H, Ohta H, Watanabe K, Yamashita H, Kimura H, Sato Y. Multiple processing forms and their biological activities of a novel angiogenesis inhibitor vasohibin. Biochem Biophys Res Commun. 2006 Apr 7;342(2):640-6. Epub 2006 Feb 13. PMID:16488400 doi:http://dx.doi.org/S0006-291X(06)00167-7
  3. ↑ Yamashita H, Abe M, Watanabe K, Shimizu K, Moriya T, Sato A, Satomi S, Ohta H, Sonoda H, Sato Y. Vasohibin prevents arterial neointimal formation through angiogenesis inhibition. Biochem Biophys Res Commun. 2006 Jul 7;345(3):919-25. doi:, 10.1016/j.bbrc.2006.04.176. Epub 2006 May 8. PMID:16707096 doi:http://dx.doi.org/10.1016/j.bbrc.2006.04.176
  4. ↑ Kimura H, Miyashita H, Suzuki Y, Kobayashi M, Watanabe K, Sonoda H, Ohta H, Fujiwara T, Shimosegawa T, Sato Y. Distinctive localization and opposed roles of vasohibin-1 and vasohibin-2 in the regulation of angiogenesis. Blood. 2009 May 7;113(19):4810-8. doi: 10.1182/blood-2008-07-170316. Epub 2009, Feb 9. PMID:19204325 doi:http://dx.doi.org/10.1182/blood-2008-07-170316
  5. ↑ Nieuwenhuis J, Adamopoulos A, Bleijerveld OB, Mazouzi A, Stickel E, Celie P, Altelaar M, Knipscheer P, Perrakis A, Blomen VA, Brummelkamp TR. Vasohibins encode tubulin detyrosinating activity. Science. 2017 Dec 15;358(6369):1453-1456. doi: 10.1126/science.aao5676. Epub 2017, Nov 16. PMID:29146869 doi:http://dx.doi.org/10.1126/science.aao5676
  6. ↑ Suzuki Y, Kobayashi M, Miyashita H, Ohta H, Sonoda H, Sato Y. Isolation of a small vasohibin-binding protein (SVBP) and its role in vasohibin secretion. J Cell Sci. 2010 Sep 15;123(Pt 18):3094-101. doi: 10.1242/jcs.067538. Epub 2010, Aug 24. PMID:20736312 doi:http://dx.doi.org/10.1242/jcs.067538
  7. ↑ Kadonosono T, Yimchuen W, Tsubaki T, Shiozawa T, Suzuki Y, Kuchimaru T, Sato Y, Kizaka-Kondoh S. Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release. Protein Sci. 2017 Mar;26(3):452-463. doi: 10.1002/pro.3089. Epub 2017 Feb 11. PMID:27879017 doi:http://dx.doi.org/10.1002/pro.3089
  8. ↑ Nieuwenhuis J, Adamopoulos A, Bleijerveld OB, Mazouzi A, Stickel E, Celie P, Altelaar M, Knipscheer P, Perrakis A, Blomen VA, Brummelkamp TR. Vasohibins encode tubulin detyrosinating activity. Science. 2017 Dec 15;358(6369):1453-1456. doi: 10.1126/science.aao5676. Epub 2017, Nov 16. PMID:29146869 doi:http://dx.doi.org/10.1126/science.aao5676

6ocf, resolution 2.10Å

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