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Article

Effect of the distal C162S mutation on the energetics of drug binding to p38alpha MAP kinase.

Archives of biochemistry and biophysics - 15 Jan 2008

Todorova Niya A, Doseeva Victoria, Ramprakash Jayanthi, Schwarz Frederick P

Abstract excerpt

The binding reactions of the inhibitor drugs, SB 203580, SKF 86002, and p38 INH.1 to the isoforms 1 and 2 splice variants of p38alpha MAP kinase and their C162S mutants, as determined from ITC measurements from 25 to 35 degrees C, are totally enthalpically driven with binding constants ranging from 10(7)M(-1) for SKF 86002 and SB 203580 to 10(9)M(-1) for p38 INH.1. Interactions of p38 INH.1 with an additional...

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Source

Identifiers

PMID: 17996717
DOI: 10.1016/j.abb.2007.10.014

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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