3C1V

The 1.5 A Crystal structure of Ca2+-bound S100A4

Summary for 3C1V

• Entry DOI: 10.2210/pdb3c1v/pdb
• Descriptor: Protein S100-A4, CALCIUM ION (3 entities in total)
• Functional Keywords: s100a4, ca2+-bound, calcium-bound, calcium binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 52924.88

Authors

Gingras, A.R.,Barsukov, I.L. (deposition date: 2008-01-24, release date: 2008-04-01, Last modification date: 2023-11-01)

Primary citation

Gingras, A.R.,Basran, J.,Prescott, A.,Kriajevska, M.,Bagshaw, C.R.,Barsukov, I.L.
Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4
Febs Lett., 582:1651-1656, 2008

PubMed 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)).

PubMed: 18435928
DOI: 10.1016/j.febslet.2008.04.017

Experimental method

X-RAY DIFFRACTION (1.5 Å)