1v8k: Difference between revisions

Revision as of 15:49, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v8k.png

Template:STRUCTURE 1v8k

The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNPThe Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP

Template:ABSTRACT PUBMED 14980225

About this StructureAbout this Structure

1V8K is a Single protein structure of sequence from Mus musculus. 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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OCA

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-'''The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP'''
+===The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14980225}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14980225}}
 ==About this Structure==
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 [[Category: Kinesin-like protein]]
 [[Category: Microtubule destabilizer]]
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