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Article

Intersubunit association induces unique allosteric dependence of the T127L CRP mutant on pH.

Biochemistry - 20 Jun 2000

Shi Y, Wang S, Schwarz F P

Abstract excerpt

The allosteric activation of the T127-->L mutant of 3',5'-cyclic adenosine monophosphate (cAMP) receptor protein (CRP) by cAMP changes from an exothermic, independent two-site binding mechanism at pH 7.0 to an endothermic, interacting two-site binding mechanism at pH 5.2, similar to that observed for CRP at pH 7.0 and 5.2. Since the T127-->L mutation at the subunit interface of the CRP dimer creates a more...

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Source

Identifiers

PMID: 10852730
DOI: 10.1021/bi000225m

Genes

CRP

Variants

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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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