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5WDH

Motor domain of human kinesin family member C1

Replaces:  2REP
Summary for 5WDH
Entry DOI10.2210/pdb5wdh/pdb
DescriptorKinesin-like protein KIFC1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordskinesin, structural genomics consortium, motor domain, adp, sgc, motor protein
Biological sourceHomo sapiens (Human)
Cellular locationNucleus : Q9BW19
Total number of polymer chains1
Total formula weight41030.12
Authors
Zhu, H.,Tempel, W.,He, H.,Shen, Y.,Wang, J.,Brothers, G.,Landry, R.,Arrowsmith, C.H.,Edwards, A.M.,Park, H.,Structural Genomics Consortium (SGC) (deposition date: 2017-07-05, release date: 2017-08-09, Last modification date: 2023-10-04)
Primary citationPark, H.W.,Ma, Z.,Zhu, H.,Jiang, S.,Robinson, R.C.,Endow, S.A.
Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.
Sci Rep, 7:15121-15121, 2017
Cited by
PubMed Abstract: Kinesin microtubule motor proteins play essential roles in division, including attaching chromosomes to spindles and crosslinking microtubules for spindle assembly. Human kinesin-14 KIFC1 is unique in that cancer cells with amplified centrosomes are dependent on the motor for viable division because of its ability to cluster centrosomes and form bipolar spindles, but it is not required for division in almost all normal cells. Screens for small molecule inhibitors of KIFC1 have yielded several candidates for further development, but obtaining structural data to determine their sites of binding has been difficult. Here we compare a previously unreported KIFC1 crystal structure with new structures of two closely related kinesin-14 proteins, Ncd and KIFC3, to determine the potential binding site of a known KIFC1 ATPase inhibitor, AZ82. We analyze the previously identified kinesin inhibitor binding sites and identify features of AZ82 that favor binding to one of the sites, the α4/α6 site. This selectivity can be explained by unique structural features of the KIFC1 α4/α6 binding site. These features may help improve the drug-like properties of AZ82 and other specific KIFC1 inhibitors.
PubMed: 29123223
DOI: 10.1038/s41598-017-14754-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.248 Å)
Structure validation

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