3ryc: Difference between revisions
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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=3ryc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ryc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ryc RCSB], [http://www.ebi.ac.uk/pdbsum/3ryc 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=3ryc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ryc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ryc RCSB], [http://www.ebi.ac.uk/pdbsum/3ryc PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/D0VWZ0_SHEEP D0VWZ0_SHEEP]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] [[http://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref> [[http://www.uniprot.org/uniprot/D0VWY9_SHEEP D0VWY9_SHEEP]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505] | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 17:47, 25 December 2014
Tubulin: RB3 stathmin-like domain complexTubulin: RB3 stathmin-like domain complex
Structural highlights
Function[D0VWZ0_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] [STMN4_RAT] Exhibits microtubule-destabilizing activity.[1] [2] [3] [D0VWY9_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505] Publication Abstract from PubMedTubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to alphabeta-tubulin is required for microtubule assembly, but whether this triggers conversion into a straighter structure is still debated. This is due, at least in part, to the lack of structural data for GTP-tubulin before assembly. Here, we report atomic-resolution crystal structures of soluble tubulin in the GDP and GTP nucleotide states in a complex with a stathmin-like domain. The structures differ locally in the neighborhood of the nucleotide. A loop movement in GTP-bound tubulin favors its recruitment to the ends of growing microtubules and facilitates its curved-to-straight transition, but this conversion has not proceeded yet. The data therefore argue for the conformational change toward the straight structure occurring as microtubule-specific contacts are established. They also suggest a model for the way the tubulin structure is modified in relation to microtubule assembly. The determinants that govern microtubule assembly from the atomic structure of GTP-tubulin.,Nawrotek A, Knossow M, Gigant B J Mol Biol. 2011 Sep 9;412(1):35-42. Epub 2011 Jul 23. PMID:21787788[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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