Title : Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions.

Pub. Date : 2003 May 23

PMID : 12742020






5 Functional Relationships(s)
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1 Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions. Calcium gelsolin Homo sapiens
2 Structural analysis of gelsolin domains 4-6 demonstrates that the two highest-affinity calcium ions that activate the molecule are in domains 5 and 6, one in each. Calcium gelsolin Homo sapiens
3 Since the disposition of the three domains is similar in different crystal environments, either free or in complex with actin, the conformation in calcium is intrinsic to active gelsolin itself. Calcium gelsolin Homo sapiens
4 The last 13 residues of domain 6 have been proposed to be a calcium-activated latch that, in the inhibited form only, links two halves of gelsolin. Calcium gelsolin Homo sapiens
5 A structural alignment of domain sequences provides a rationale to understand why the two calcium sites found here have the highest affinity amongst the five different candidate sites found in other gelsolin structures. Calcium gelsolin Homo sapiens