4eb6 | pdb_00004eb6

Tubulin-Vinblastine: Stathmin-like complex

spinqualitylabelsall models 4eb6, resolution 3.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4eb6 is a 5 chain structure with sequence from Ovis aries and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, GTP, MG, SO4, VLB Related: 3ut5 Gene: Stmn4 (Rattus norvegicus) Resources: FirstGlance, OCA, RCSB, PDBsum 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. [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 PubMed Vinca-domain ligands are compounds that bind to tubulin at its inter-heterodimeric interface and favour heterogeneous protofilament-like assemblies, giving rise to helices and rings. This is the basis for their inhibition of microtubule assembly, for their antimitotic activities and for their use in anticancer chemotherapy. Ustiloxins are vinca-domain ligands with a well established total synthesis. A 2.7 A resolution structure of ustiloxin D bound to the vinca domain embedded in the complex of two tubulins with the stathmin-like domain of RB3 (T(2)R) has been determined. This finding precisely defines the interactions of ustiloxins with tubulin and, taken together with structures of other vinca-ligand complexes, allows structure-based suggestions to be made for improved activity. These comparisons also provide a rationale for the large-scale polymorphism of the protofilament-like assemblies mediated by vinca-domain ligands based on local differences in their interactions with the two tubulin heterodimers constituting their binding site. Structural plasticity of tubulin assembly probed by vinca-domain ligands.,Ranaivoson FM, Gigant B, Berritt S, Joullie M, Knossow M Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):927-34. Epub 2012 Jul 7. PMID:22868758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tubulin

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