Gelsolin

Function

Gelsolin (GLS) is a protein regulator of actin assembly and disassembly^[1]. Binding of Ca+2 ion to GLS induces conformational change which enables it to bind actin.

Structural highlights

GLS contains 6 homologous domains S1 to S6. The human GLS domains span residues: 15-135, 136-248, 249-367, 394-513, 514-619 and 620-734. . The ^[2].

3D Structures of gelsolin

Gelsolin 3D structures

Human gelsolin S4-S6 (gold) complex with actin (cyan), ATP and Ca+2 ion (green) (PDB entry 1h1v)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Sun HQ, Yamamoto M, Mejillano M, Yin HL. Gelsolin, a multifunctional actin regulatory protein. J Biol Chem. 1999 Nov 19;274(47):33179-82. PMID:10559185
↑ Choe H, Burtnick LD, Mejillano M, Yin HL, Robinson RC, Choe S. The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex. J Mol Biol. 2002 Dec 6;324(4):691-702. PMID:12460571

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Alexander Berchansky, Michal Harel, Jaime Prilusky

[1] Sun HQ, Yamamoto M, Mejillano M, Yin HL. Gelsolin, a multifunctional actin regulatory protein. J Biol Chem. 1999 Nov 19;274(47):33179-82. PMID:10559185

[2] Choe H, Burtnick LD, Mejillano M, Yin HL, Robinson RC, Choe S. The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex. J Mol Biol. 2002 Dec 6;324(4):691-702. PMID:12460571

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