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Article

Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.

Biophysical journal - 11 Apr 2017

Sukomon Nattakan, Widom Joanne, Borbat Peter P, Freed Jack H, Crane Brian R

Abstract excerpt

HAMP domains are dimeric, four-helix bundles that transduce conformational signals in bacterial receptors. Genetic studies of the Escherichia coli serine receptor (Tsr) provide an opportunity to understand HAMP conformational behavior in terms of functional output. To increase its stability, the Tsr HAMP domain was spliced into a poly-HAMP unit from the Pseudomonas aeruginosa Aer2 receptor. Within the chimera,...

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Identifiers

PMID: 28402881
DOI: 10.1016/j.bpj.2017.02.037
PMCID: PMC5390053

Genes

HAMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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