6j4p: Difference between revisions
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<StructureSection load='6j4p' size='340' side='right'caption='[[6j4p]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6j4p' size='340' side='right'caption='[[6j4p]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6j4p]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6j4p]] is a 2 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=6J4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J4P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.599Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BJL:N-[(3R)-4-ethoxy-3-hydroxy-4-oxobutanoyl]-L-tyrosine'>BJL</scene></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=6j4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j4p OCA], [https://pdbe.org/6j4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j4p RCSB], [https://www.ebi.ac.uk/pdbsum/6j4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j4p ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 6j4p" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6j4p" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bao H]] | |||
[[Category: Bao | [[Category: Huang H]] | ||
[[Category: Huang | [[Category: Wang N]] | ||
[[Category: Wang | |||
Latest revision as of 12:59, 22 November 2023
Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implicationsStructural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications
Structural highlights
FunctionPublication Abstract from PubMedVasohibins 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 AlsoReferences
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