Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4.
FEBS Lett
; 582(12): 1651-6, 2008 May 28.
Article
em En
| MEDLINE
| ID: mdl-18435928
ABSTRACT
S100A4 takes part in control of tumour cell migration and contributes to metastatic spread in in vivo models. In the active dimeric Ca(2+)-bound state it interacts with multiple intracellular targets. Conversely, oligomeric forms of S100A4 are linked with the extracellular function of this protein. We report the 1.5A X-ray crystal structure of Ca(2+)-bound S100A4 and use it to identify the residues involved in target recognition and to derive a model of the oligomeric state. We applied stopped-flow analysis of tyrosine fluorescence to derive kinetics of S100A4 activation by Ca(2+) (k(on)=3.5 microM(-1)s(-1), k(off)=20s(-1)).
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1
Base de dados:
MEDLINE
Assunto principal:
Proteínas S100
/
Cálcio
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article