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Gelsolin
From Proteopedia
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| - | + | <StructureSection load='1h1v' size='350' side='right' caption='Human gelsolin S4-S6 (gold) complex with actin (cyan), ATP and Ca+2 ion (green) (PDB entry [[1h1v]])' scene='41/410297/Cv/3'> | |
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| - | + | == Function == | |
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| - | + | [[Gelsolin]] (GLS) is a protein regulator of actin assembly and disassembly<ref>PMID:10559185</ref>. 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. <scene name='41/410297/Cv/6'>S4-S6 are shown</scene>. The <scene name='41/410297/Cv/7'>binding site of Ca+2 ion includes Glu, Asp and 2 carbonyl oxygens</scene><ref>PMID:12460571</ref>. |
| - | + | == 3D Structures of gelsolin == | |
| + | [[Gelsolin 3D structures]] | ||
| - | + | </StructureSection> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | [[Category:Topic Page]] | |
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References
- ↑ 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
