Gelsolin

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== Structural highlights ==
== Structural highlights ==
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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/4'>S4-S6 are shown</scene>. The <scene name='41/410297/Cv/5'>binding site of Ca+2 ion includes Glu, Asp and 2 carbonyl oxygens</scene><ref>PMID:12460571</ref>.
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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>.
</StructureSection>
</StructureSection>
== 3D Structures of GLS ==
== 3D Structures of GLS ==

Revision as of 10:28, 31 March 2019

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

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3D Structures of GLS

Updated on 31-March-2019

References

  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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Michal Harel, Alexander Berchansky, Jaime Prilusky

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