Different cation binding to the I domains of alpha1 and alpha2 integrins: implication of the binding site structure

T Obsil1, K Hofbauerová, E Amler

  • 1Department of Physical and Macromolecular Chemistry, Faculty of Sciences, Charles University, Hlavova 8/2030, 128 40, Prague, Czech Republic. obsil@biomed.cas.cz

FEBS Letters
|September 3, 1999
PubMed

In the present work, we studied the interactions of recombinant alpha1 and alpha2 integrin I domains with cations Tb(3+), Mn(2+), Mg(2+) and Ca(2+). We observed that alpha1 and alpha2 I domains bind these cations with significantly different characteristics. The binding of Mg(2+) by the alpha1 I domain was accompanied by significant changes of tryptophan fluorescence which could be interpreted as a conformational change. Comparison of the alpha1 integrin I domain structure obtained by comparative modeling with a known structure of the alpha2 integrin I domain shows distinct differences in the metal ion binding sites which could explain the differences in cation binding.

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