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| <StructureSection load='6j4v' size='340' side='right'caption='[[6j4v]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6j4v' size='340' side='right'caption='[[6j4v]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6j4v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Homo Homo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J4V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j4v]] is a 3 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=6J4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J4V FirstGlance]. <br> |
- | </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=PO4:PHOSPHATE+ION'>PO4</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]] 2.1Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VASH2, VASHL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SVBP, CCDC23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
- | <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'>[https://proteopedia.org/fgij/fg.htm?mol=6j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j4v OCA], [https://pdbe.org/6j4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j4v RCSB], [https://www.ebi.ac.uk/pdbsum/6j4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j4v 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=6j4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j4v OCA], [http://pdbe.org/6j4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j4v RCSB], [http://www.ebi.ac.uk/pdbsum/6j4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j4v ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[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> | + | [https://www.uniprot.org/uniprot/VASH2_HUMAN VASH2_HUMAN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6j4v" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6j4v" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] |
| + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Homo]] | + | [[Category: Homo sapiens]] |
- | [[Category: Human]]
| + | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Tubulinyl-Tyr carboxypeptidase]]
| + | [[Category: Bao H]] |
- | [[Category: Bao, H]] | + | [[Category: Huang H]] |
- | [[Category: Huang, H]] | + | [[Category: Wang N]] |
- | [[Category: Wang, N]] | + | |
- | [[Category: Carboxypeptidase]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Microtubule]]
| + | |
- | [[Category: Tubulin]]
| + | |
| Structural highlights
Function
VASH2_HUMAN
Publication Abstract from PubMed
Vasohibins are tubulin tyrosine carboxypeptidases that are important in neuron physiology. We examined the crystal structures of human vasohibin 1 and 2 in complex with small vasohibin-binding protein (SVBP) in the absence and presence of different inhibitors and a C-terminal alpha-tubulin peptide. In combination with functional data, we propose that SVBP acts as an activator of vasohibins. An extended groove and a distinctive surface residue patch of vasohibins define the specific determinants for recognizing and cleaving the C-terminal tyrosine of alpha-tubulin and for binding microtubules, respectively. The vasohibin-SVBP interaction and the ability of the enzyme complex to associate with microtubules regulate axon specification of neurons. Our results define the structural basis of tubulin detyrosination by vasohibins and show the relevance of this process for neuronal development. Our findings offer a unique platform for developing drugs against human conditions with abnormal tubulin tyrosination levels, such as cancer, heart defects and possibly brain disorders.
Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme complex.,Wang N, Bosc C, Ryul Choi S, Boulan B, Peris L, Olieric N, Bao H, Krichen F, Chen L, Andrieux A, Olieric V, Moutin MJ, Steinmetz MO, Huang H Nat Struct Mol Biol. 2019 Jul;26(7):571-582. doi: 10.1038/s41594-019-0241-y. Epub, 2019 Jun 24. PMID:31235911[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wang N, Bosc C, Ryul Choi S, Boulan B, Peris L, Olieric N, Bao H, Krichen F, Chen L, Andrieux A, Olieric V, Moutin MJ, Steinmetz MO, Huang H. Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme complex. Nat Struct Mol Biol. 2019 Jul;26(7):571-582. doi: 10.1038/s41594-019-0241-y. Epub, 2019 Jun 24. PMID:31235911 doi:http://dx.doi.org/10.1038/s41594-019-0241-y
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