Different cation binding to the I domains of α1 and α2 integrins: implication of the binding site structure

FEBS Letters

Hofbauerová, Kateřina²  Obšil, Tomáš¹  Teisinger, Jan²  Amler, Evžen² 

[1]Department of Physical and Macromolecular Chemistry, Faculty of Sciences, Charles University, Hlavova 8/2030, 128 40 Prague, Czech Republic

[2]Institute of Physiology, Czech Academy of Sciences, Vı́denská 1083, 142 20 Prague, Czech Republic

关键词: Integrin;    I domain;    Cation binding;    Terbium fluorescence;    Comparative modeling;    GST;    glutathione S-transferase;    MIDAS;    metal ion-dependent adhesion site;   

DOI  :  10.1016/S0014-5793(99)01063-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the present work, we studied the interactions of recombinant α1 and α2 integrin I domains with cations Tb³⁺, Mn²⁺, Mg²⁺ and Ca²⁺. We observed that α1 and α2 I domains bind these cations with significantly different characteristics. The binding of Mg²⁺ by the α1 I domain was accompanied by significant changes of tryptophan fluorescence which could be interpreted as a conformational change. Comparison of the α1 integrin I domain structure obtained by comparative modeling with a known structure of the α2 integrin I domain shows distinct differences in the metal ion binding sites which could explain the differences in cation binding.

【 授权许可】

Unknown