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Article

The HAMP domain structure implies helix rotation in transmembrane signaling.

Cell - 8 Sept 2006

Hulko Michael, Berndt Franziska, Gruber Markus, Linder Jürgen U, Truffault Vincent, Schultz Anita, Martin Jörg, Schultz Joachim E, Lupas Andrei N, Coles Murray

Abstract excerpt

HAMP domains connect extracellular sensory with intracellular signaling domains in over 7500 proteins, including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. The solution structure of an archaeal HAMP domain shows a homodimeric, four-helical, parallel coiled coil with unusual interhelical packing, related to the canonical packing by rotation of the helices. This suggests a model...

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Share to Adenylyl Cyclases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Nuclear Magnetic Resonance, Biomolecular

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Source

Identifiers

PMID: 16959572
DOI: 10.1016/j.cell.2006.06.058

Genes

HAMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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