6nvq

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m (Protected "6nvq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6nvq is ON HOLD
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==Crystal structure of the VASH1-SVBP complex==
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<StructureSection load='6nvq' size='340' side='right'caption='[[6nvq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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Authors: Adamopoulos, A., Perrakis, A., Heidebrecht, T.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6nvq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NVQ FirstGlance]. <br>
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Description: Crystal structure of the VASH1-SVBP complex
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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[[Category: Unreleased Structures]]
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<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>
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<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=6nvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nvq OCA], [http://pdbe.org/6nvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nvq RCSB], [http://www.ebi.ac.uk/pdbsum/6nvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nvq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Tubulinyl-Tyr carboxypeptidase]]
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[[Category: Adamopoulos, A]]
[[Category: Heidebrecht, T]]
[[Category: Heidebrecht, T]]
[[Category: Perrakis, A]]
[[Category: Perrakis, A]]
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[[Category: Adamopoulos, A]]
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[[Category: Hydrolase]]
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[[Category: Tyrosine carboxypeptidase]]

Revision as of 06:53, 23 May 2019

Crystal structure of the VASH1-SVBP complex

PDB ID 6nvq

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