Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Transport by ABC proteins requires a cycle of ATP-driven conformational changes of the nucleotide binding domains (NBDs). We compare three molecular dynamics simulations of dimeric MJ0796: with ATP was present at both NBDs; with ATP at one NBD but ADP at the other; and without any bound ATP. In the simulation with ATP present at both NBDs, the dimeric protein interacts with the nucleotides in a symmetrical manner. However, if ADP is present at one binding site then both NBD-NBD and protein-ATP interactions are enhanced at the opposite site.

Original publication

DOI

10.1016/j.febslet.2005.06.027

Type

Journal article

Journal

FEBS Lett

Publication Date

01/08/2005

Volume

579

Pages

4193 - 4199

Keywords

ATP-Binding Cassette Transporters, Adenosine Diphosphate, Adenosine Triphosphate, Binding Sites, Computational Biology, Crystallography, X-Ray, Dimerization, Models, Molecular, Protein Binding, Protein Conformation