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

FEBS Letters

Kuźnicki, Jacek²  Finn, Bryan E¹  Forsén, Sture¹  Groves, Patrick² 

[1] Department of Physical Chemistry 2, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, S-221 00 Lund, Sweden;Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland

关键词: S100;    Calcium-binding protein;    Protein structure;    Target protein binding;    CSI;    chemical shift index;    NOE;    nuclear Overhauser effect spectroscopy crosspeak;    P43G;    a calbindin D9k mutant;    P43MG;    a calbindin D9k mutant where residue P43 is replaced with the sequence M43G43a;   

DOI  :  10.1016/S0014-5793(97)01535-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown