Title : Identification of a dimeric intermediate in the unfolding pathway for the calcium-binding protein S100B.

Pub. Date : 2008 Oct 17

PMID : 18706914






6 Functional Relationships(s)
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1 Identification of a dimeric intermediate in the unfolding pathway for the calcium-binding protein S100B. Calcium S100 calcium binding protein B Homo sapiens
2 One member of this family, S100B, is a homodimeric protein shown to control the assembly of several cytoskeletal proteins and regulate phosphorylation events in a calcium-sensitive manner. Calcium S100 calcium binding protein B Homo sapiens
3 Calcium binding to S100B causes a conformational change involving movement of helix III in the second calcium-binding site (EF2) that exposes a hydrophobic surface enabling interactions with other proteins such as tubulin and Ndr kinase. Calcium S100 calcium binding protein B Homo sapiens
4 Calcium binding to S100B causes a conformational change involving movement of helix III in the second calcium-binding site (EF2) that exposes a hydrophobic surface enabling interactions with other proteins such as tubulin and Ndr kinase. Calcium S100 calcium binding protein B Homo sapiens
5 In this work, we have examined the guanidine hydrochloride (GuHCl)-induced unfolding of dimeric calcium-free S100B. Calcium S100 calcium binding protein B Homo sapiens
6 Together these observations show that calcium-free S100B unfolds via a dimeric intermediate. Calcium S100 calcium binding protein B Homo sapiens