Proteins in Motion

Some membrane receptors undergo conformational changes after binding their ligand, generating a signal transduction cascade that results in a change in gene expression. But how the motion of proteins is translated into altered signaling is not known. In their Perspective, [Gerstein and Chothia][1] describe how transmembrane helices in a bacterial membrane receptor slide over each other in a piston-like motion ([ Ottemann et al .][2]). They discuss how these results fit with current models of transmembrane conformational changes and signaling and whether these findings are likely to be applicable to other types of transmembrane proteins. [1]: http://www.sciencemag.org/cgi/content/full/285/5434/1682 [2]: http://www.sciencemag.org/cgi/content/short/285/5434/1751

[1]  D E Koshland,et al.  A piston model for transmembrane signaling of the aspartate receptor. , 1999, Science.

[2]  Sung-Hou Kim,et al.  Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor , 1999, Nature.

[3]  E. Perozo,et al.  Structural rearrangements underlying K+-channel activation gating. , 1999, Science.

[4]  R. Henderson,et al.  Protein conformational changes in the bacteriorhodopsin photocycle. , 1999, Journal of molecular biology.

[5]  M. Gerstein Patterns of protein‐fold usage in eight microbial genomes: A comprehensive structural census , 1998, Proteins.

[6]  M. Gerstein,et al.  A database of macromolecular motions. , 1998, Nucleic acids research.

[7]  G. Heijne,et al.  Genome‐wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms , 1998, Protein science : a publication of the Protein Society.

[8]  J. Beckwith,et al.  How many membrane proteins are there? , 1998, Protein science : a publication of the Protein Society.

[9]  A T Brünger,et al.  Are there dominant membrane protein families with a given number of helices? , 1997, Proteins.

[10]  James H. Prestegard,et al.  A Transmembrane Helix Dimer: Structure and Implications , 1997, Science.

[11]  A. Lesk,et al.  Structural mechanisms for domain movements in proteins. , 1994, Biochemistry.

[12]  D. Engelman,et al.  Specificity and promiscuity in membrane helix interactions , 1994, Quarterly Reviews of Biophysics.

[13]  D. Koshland,et al.  Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[14]  Cyrus Chothia,et al.  Transmission of conformational change in insulin , 1983, Nature.

[15]  F. Richards The interpretation of protein structures: total volume, group volume distributions and packing density. , 1974, Journal of molecular biology.

[16]  N. Unwin The Nicotinic Acetylcholine Receptor of theTorpedoElectric Ray , 1998 .