5lxt

Tubulin-Discodermolide complex

spinqualitylabelsall models 5lxt, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lxt is a 6 chain structure with sequence from Bos taurus, Gallus gallus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 7AK, ACP, CA, GDP, GTP, MES, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E1BQ43_CHICK Publication Abstract from PubMed Microtubule-stabilizing agents (MSAs) are widely used in chemotherapy. Here, using X-ray crystallography we describe the detailed binding modes of two potent MSAs, (+)-discodermolide (DDM) and the DDM-paclitaxel-hybrid KS-1-199-32, in the taxane pocket of ss-tubulin. Both compounds bind in a very similar hairpin conformation as previously observed in solution. However, they differentially stabilize the M-loop of ss-tubulin: KS-1-199-32 induces an M-loop helical conformation that is not observed for DDM. In the context of the microtubule structure, both MSAs connect the ss-tubulin helices H6 and H7 and loop S9-S10 with the M-loop, which is similar to the structural effects elicited by epothilone A, but distinct from paclitaxel. Together, our data rationalize a differential binding mechanism of DDM and KS-1-199-32 on tubulin. Structural Basis of Microtubule Stabilization by Discodermolide.,Prota AE, Bargsten K, Redondo M, Smith Iii AB, Yang CH, McDaid HM, Paterson I, Horwitz SB, Diaz JF, Steinmetz MO Chembiochem. 2017 Feb 16. doi: 10.1002/cbic.201600696. PMID:28207984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Stathmin-4 3D structures Tubulin tyrosine ligase

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