HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 2, 1267-1275, January 12, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/2/1267    most recent M007169200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kozielski, F. Articles by Koch, M. H.J. Search for Related Content PubMed PubMed Citation Articles by Kozielski, F. Articles by Koch, M. H.J. Social Bookmarking                      What's this?

The Overall Conformation of Conventional Kinesins Studied by Small Angle X-ray and Neutron Scattering^*

Frank Kozielski^§, Dmitri Svergun^¶, Giuseppe Zaccaï^**, Richard H. Wade, and Michel H.J. Koch^¶

From the  Laboratoire de Microscopie Electronique Structurale and ^** Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale (CEA 47 CNRS), 41, rue Jules Horowitz, 38027 Grenoble Cedex 01, France, ^¶ European Molecular Biology Laboratory, EMBL c/o DESY, Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany,  Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59 117333, Russia, and the  Institut-Laue-Langevin B. P. 156 F-38042 Grenoble Cedex 9, France

The quaternary structures of several monomeric and dimeric kinesin constructs from Homo sapiens and Drosophila melanogaster were analyzed using small angle x-ray and neutron scattering. The experimental scattering curves of these proteins were compared with simulated scattering curves calculated from available crystallographic coordinates. These comparisons indicate that the overall conformations of the solution structures of D. melanogaster and H. sapiens kinesin heavy chain dimers are compatible with the crystal structure of dimeric kinesin from Rattus norvegicus. This suggests that the unusual asymmetric conformation of dimeric kinesin in the microtubule-independent ADP state is likely to be a general feature of the kinesin heavy chain subfamily. An intermediate length Drosophila construct (365 residues) is mostly monomeric at low protein concentration whereas at higher concentrations it is dimeric with a tendency to form higher oligomers.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				D. A. Skoufias, S. DeBonis, Y. Saoudi, L. Lebeau, I. Crevel, R. Cross, R. H. Wade, D. Hackney, and F. Kozielski S-Trityl-L-cysteine Is a Reversible, Tight Binding Inhibitor of the Human Kinesin Eg5 That Specifically Blocks Mitotic Progression J. Biol. Chem., June 30, 2006; 281(26): 17559 - 17569. [Abstract] [Full Text] [PDF]

				D. I. Svergun, G. Zaccai, M. Malfois, R. H. Wade, M. H. J. Koch, and F. Kozielski Conformation of the Drosophila Motor Protein Non-claret Disjunctional in Solution from X-ray and Neutron Scattering J. Biol. Chem., June 29, 2001; 276(27): 24826 - 24832. [Abstract] [Full Text] [PDF]