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

Sammanfattning

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.

Nyckelord

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

Publicerad i

FEBS LETTERS
1998, volym: 421, nummer: 3, sidor: 175-179

SLU författare

• Finn, Bryan

  • Lunds Universitet

UKÄ forskningsämne

Molekylärbiologi
Biokemi

Publikationens identifierare

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

Permanent länk till denna sida (URI)

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