1v8k
The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP
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OverviewOverview
Unlike other kinesins, middle motor domain-type kinesins depolymerize the, microtubule from its ends. To elucidate its mechanism, we solved the X-ray, crystallographic structure of KIF2C, a murine member of this family. Three, major class-specific features were identified. The class-specific, N-terminal neck adopts a long and rigid helical structure extending out, vertically into the interprotofilament groove. This structure explains its, dual roles in targeting to the end of the microtubule and in, destabilization of the lateral interaction of the protofilament. The loop, L2 forms a unique finger-like structure, long and rigid enough to reach, the next tubulin subunit to stabilize the peeling of the protofilament., The open conformation of the switch I loop could be reversed by the shift, of the microtubule binding L8 loop, suggesting its role as the sensor to, trigger ATP hydrolysis. Mutational analysis supports these structural, implications.
About this StructureAbout this Structure
1V8K is a Single protein structure of sequence from Mus musculus with MG and ANP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops., Ogawa T, Nitta R, Okada Y, Hirokawa N, Cell. 2004 Feb 20;116(4):591-602. PMID:14980225
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