Loop L5 acts as a conformational latch in the mitotic kinesin Eg5

Journal of Biological Chemistry

Volumn 286, Issue 7, 2011, Pages 5242-5253

  Behnke Parks, William M ^a   Vendome, Jeremie ^a   Honig, Barry ^a   Maliga, Zoltan ^b   Moores, Carolyn ^c   Rosenfeld, Steven S ^d  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b MAX PLANCK INSTITUTE OF MOLECULAR CELL BIOLOGY AND GENETICS   (Germany)

^c UNIVERSITY OF LONDON   (United Kingdom)

^d College of Physicians and Surgeons ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; CATALYTIC SITES; CONFORMATIONAL CHANGE; CRYO-ELECTRON MICROSCOPY; FORCE GENERATION; KEY ELEMENTS; KINESIN MOTORS; KINESINS; MICROTUBULE-BINDING DOMAINS; MITOTIC KINESIN EG5; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR MOTORS; NUCLEOTIDE-BINDING SITES; PROLINE RESIDUES; SITE DIRECTED MUTAGENESIS; STRUCTURAL CHANGE; STRUCTURAL ELEMENTS; STRUCTURAL MOTIFS; TRANSIENT STATE KINETICS;

AMINO ACIDS; NUCLEOTIDES;

MOLECULAR DYNAMICS;

ADENOSINE TRIPHOSPHATE; KINESIN; KINESIN EG5; NUCLEOTIDE BINDING PROTEIN; PROLINE; PROTEIN L5; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; ENZYME ACTIVE SITE; ENZYME REGULATION; MICROTUBULE ASSEMBLY; MITOSIS; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RESIDUE ANALYSIS; SITE DIRECTED MUTAGENESIS; STEADY STATE; STRUCTURE ANALYSIS;

ANIMALS; CATALYTIC DOMAIN; COMPUTER SIMULATION; HUMANS; KINESIN; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY;

EID: 79953129078     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.192930     Document Type: Article

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