Signaling by transmembrane proteins shifts gears.

Cell ·Vol. 126 ·No. 5 ·2006-09-08 ·Pages 829-31

Inouye M

Abstract

The HAMP domain is present in a large number of transmembrane proteins in prokaryotes including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. In this issue of Cell, Hulko et al. (2006) report the NMR structure of a HAMP domain and present data suggesting that it transduces signals through a simple rotation of its four-helix parallel coiled coil.

MeSH Terms

Archaeal Proteins/chemistry,metabolism Archaeoglobus fulgidus/genetics,metabolism Dimerization Histidine Kinase Membrane Proteins/chemistry,metabolism Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Kinases/chemistry,metabolism Protein Structure, Secondary Protein Structure, Tertiary Receptors, Cell Surface/chemistry,metabolism Signal Transduction

Chemicals

Archaeal Proteins Membrane Proteins Receptors, Cell Surface Protein Kinases Histidine Kinase

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Inouye Masayori

Department of Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA. inouye@umdnj.edu

Article Info

Journal

Cell

Abbr.

Cell

ISSN

0092-8674

DOI

10.1016/j.cell.2006.08.024

inouye@umdnj.edu

Published

2006-09-08

Pages

829-31

Language

English

Region

United States

NLM ID

0413066

Subset

Corrections

CommentOn

PMID: 16959572

External Links

PubMed source DOI: 10.1016/j.cell.2006.08.024 View journal details

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