4cqi

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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=4cqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cqi RCSB], [http://www.ebi.ac.uk/pdbsum/4cqi PDBsum]</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=4cqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cqi RCSB], [http://www.ebi.ac.uk/pdbsum/4cqi PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tubulin-binding cofactor A (TBCA) participates in microtubule formation, a key process in eukaryotic biology to create the cytoskeleton. There is little information on how TBCA might interact with beta-tubulin en route to microtubule biogenesis. To address this, the protozoan Leishmania major was targeted as a model system. The crystal structure of TBCA and comparisons with three orthologous proteins are presented. The presence of conserved features infers that electrostatic interactions that are likely to involve the C-terminal tail of beta-tubulin are key to association. This study provides a reagent and template to support further work in this area.
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The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly.,Barrack KL, Fyfe PK, Hunter WN Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):539-46. doi:, 10.1107/S2053230X15000990. Epub 2015 Apr 21. PMID:25945706<ref>PMID:25945706</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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Revision as of 06:30, 20 May 2015

Crystal structure of recombinant tubulin-binding cofactor A (TBCA) from Leishmania major

4cqi, resolution 1.90Å

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