Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity.

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Article

Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity.

The Journal of biological chemistry - 15 Jun 1991

Treviño C L, Boschi J M, Henzl M T

Abstract excerpt

Despite striking sequence homology with rat parvalbumin, oncomodulin exhibits much lower affinity for Ca2+ ion. We are attempting to identify the structural basis for this difference by systematically substituting the parvalbumin residue for the oncomodulin residue at points of nonidentity. In th...

Topics

Amino Acid Sequence
Animals
Binding Sites
Calcium
Calcium-Binding Proteins
Genetic Variation
Hydrogen-Ion Concentration
Kinetics
Mutagenesis, Site-Directed
Neoplasm Proteins
Parvalbumins
Protein Conformation
Rats
Sequence Homology, Nucleic Acid

Source

Open in PubMed

Identifiers

PMID: 2040635

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2040635-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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