1v8j: Difference between revisions
New page: left|200px<br /><applet load="1v8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v8j, resolution 3.24Å" /> '''The Crystal Structur... |
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[[Image:1v8j.jpg|left|200px]]<br /><applet load="1v8j" size=" | [[Image:1v8j.jpg|left|200px]]<br /><applet load="1v8j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1v8j, resolution 3.24Å" /> | caption="1v8j, resolution 3.24Å" /> | ||
'''The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-ADP'''<br /> | '''The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-ADP'''<br /> | ||
==Overview== | ==Overview== | ||
Unlike other kinesins, middle motor domain-type kinesins depolymerize the | 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 Structure== | ==About this Structure== | ||
1V8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1V8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V8J OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: microtubule destabilizer]] | [[Category: microtubule destabilizer]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:37 2008'' |
Revision as of 16:32, 21 February 2008
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The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-ADP
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
1V8J is a Single protein structure of sequence from Mus musculus with and 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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