A model for target protein binding to calcium-activated S100 dimers

Abstract

S100 proteins are a family of dimeric calcium-binding proteins implicated in several cancers and neurological diseases. Calbindin D-9k is an unusual monomeric member of the S100 family. A calbindin D-9k mutant containing a novel calcium-induced helix is characterized. Based on sequence comparison, this helix could be a component of other S100 proteins and a factor in target protein binding. The origin of structural differences between three reported apo S100 dimer structures is verified. We conclude that the differences are a result of modeling rather than a function of different target binding properties. A mechanism for target protein binding is suggested. (C) 1998 Federation of European Biochemical Societies.

Keywords

S100; calcium-binding protein; protein structure; target protein binding

Published in

FEBS LETTERS
1998, volume: 421, number: 3, pages: 175-179

SLU Authors

• Finn, Bryan

  • Lund University

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication identifier

• DOI: https://doi.org/10.1016/S0014-5793(97)01535-4

Permanent link to this page (URI)

https://res.slu.se/id/publ/132595