Oligomerization and divalent ion binding properties of the S100P protein: a Ca2+/Mg2+-switch model.

doi:10.1006/jmbi.1998.2116

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Article

Oligomerization and divalent ion binding properties of the S100P protein: a Ca2+/Mg2+-switch model.

Journal of molecular biology - 30 Oct 1998

Gribenko A V, Makhatadze G I

Abstract excerpt

S100P is a 95 amino acid residue protein which belongs to the S100 family of proteins containing two putative EF-hand Ca2+-binding motifs. In order to characterize conformational properties of S100P in the presence and absence of divalent cations (Ca2+, Mg2+ and Zn2+) in solution, we have analyze...

Topics

Amino Acid Sequence
Calbindins
Calcium
Calcium-Binding Proteins
Chromatography, Gel
Circular Dichroism
Magnesium
Models, Chemical
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Neoplasm Proteins

Protein Conformation

S100 Calcium Binding Protein G

S100 Proteins

Sequence Homology, Amino Acid

Spectrometry, Fluorescence

Source

Open in PubMed

Identifiers

PMID: 9784376
DOI: 10.1006/jmbi.1998.2116

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9784376-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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