Abstract:
:An extensive computational analysis of available sequence and crystal structure data was used to identify functionally important residue interactions within the motor domain of the kinesin molecular motor. Principal component analysis revealed that all current kinesin crystal structures reside in one of two main conformations, which differ at the active site, and in the position of a microtubule-binding sub-domain relative to a rigid central core. This sub-domain consists of secondary structure elements alpha4-loop12-alpha5-loop13 and contains a conserved hydrophilic surface patch that may be involved in strong binding to microtubules. A hinge point for the sub-domain motion lies near a conserved glycine at position 292. Statistical coupling analysis revealed a network of co-evolving positions that link this region to the nucleotide-binding site, via a highly conserved histidine in the switch I loop. The data are consistent with a model in which the nucleotide status of the active site shifts kinesin between weak and strong binding conformations via reconfiguration of the identified sub-domain. Our data provide a statistically supported framework for further examination of this and other structure-function relationships in the kinesin family.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Grant BJ,McCammon JA,Caves LS,Cross RAdoi
10.1016/j.jmb.2007.02.049subject
Has Abstractpub_date
2007-05-18 00:00:00pages
1231-48issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(07)00230-6journal_volume
368pub_type
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