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Title: Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4.
Authors: Gingras, AR
Basran, J
Prescott, A
Kriajevska, M
Bagshaw, CR
Barsukov, IL
First Published: 28-May-2008
Citation: FEBS LETT, 2008, 582 (12), pp. 1651-1656
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)).
DOI Link: 10.1016/j.febslet.2008.04.017
ISSN: 0014-5793
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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