3UT5
Tubulin-Colchicine-Ustiloxin: Stathmin-like domain complex
Summary for 3UT5
| Entry DOI | 10.2210/pdb3ut5/pdb |
| Related PRD ID | PRD_000814 |
| Descriptor | Tubulin alpha chain, Tubulin beta chain, Stathmin-4, ... (10 entities in total) |
| Functional Keywords | microtubules, tubulin, vinca domain, ustiloxin, stathmin, structural protein, structural protein-inhibitor complex, structural protein/inhibitor |
| Biological source | Rattus norvegicus (rat) More |
| Cellular location | Golgi apparatus: P63043 |
| Total number of polymer chains | 6 |
| Total formula weight | 220989.69 |
| Authors | Ranaivoson, F.M.,Gigant, B.,Knossow, M. (deposition date: 2011-11-25, release date: 2012-08-01, Last modification date: 2024-11-06) |
| Primary citation | Ranaivoson, F.M.,Gigant, B.,Berritt, S.,Joullie, M.,Knossow, M. Structural plasticity of tubulin assembly probed by vinca-domain ligands. Acta Crystallogr.,Sect.D, 68:927-934, 2012 Cited by PubMed Abstract: 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 Å 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. PubMed: 22868758DOI: 10.1107/S0907444912017143 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.73 Å) |
Structure validation
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