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Gelsolin

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<StructureSection load='1h1v' size='350' side='right' caption='Human gelsolin G4-G6 (gold) complex with actin (cyan), ATP and Ca+2 ion (green) (PDB entry [[1h1v]])' scene='41/410297/Cv/3'>
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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'>
__TOC__
__TOC__
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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GLS contains 6 homologous domains G1 to G6. 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'>G4-G6 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/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>.
</StructureSection>
</StructureSection>
== 3D Structures of GLS ==
== 3D Structures of GLS ==
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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* GLS
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* GLS residues 1-782
**[[3ffn]] – hGLS – human <br />
**[[3ffn]] – hGLS – human <br />
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**[[2x1o]], [[2x1p]], [[2x1q]] – GLS nanobody - Llama
**[[2x1o]], [[2x1p]], [[2x1q]] – GLS nanobody - Llama
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* GLS domains G1-G3
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* GLS domain S1 residues 51-178
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+
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**[[3ffk]] – hGLS +actin <br />
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-
**[[1rgi]] - hoGLS +actin <br />
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-
 
+
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* GLS domains G4-G6
+
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+
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**[[1h1v]] - hGLS +actin + Ca + ATP<br />
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-
**[[1nph]] - mGLS +Ca – mouse<br />
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-
 
+
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* GLS domain G1
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 +
**[[5h3m]], [[5h3n]] – hGLS – NMR<br />
**[[2ff3]] - hGLS +N-WASP+actin<br />
**[[2ff3]] - hGLS +N-WASP+actin<br />
**[[2ff6]] - hGLS +Ciboulot domain 2+actin<br />
**[[2ff6]] - hGLS +Ciboulot domain 2+actin<br />
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**[[1d4x]] - hGLS +CeActin+Mg-ATP – ''Caenorhabditis elegans''<br />
**[[1d4x]] - hGLS +CeActin+Mg-ATP – ''Caenorhabditis elegans''<br />
**[[1esv]] - hGLS +rActin+latrunculin – rabbit<br />
**[[1esv]] - hGLS +rActin+latrunculin – rabbit<br />
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**[[1eqy]] - hGLS +rActin<br />
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**[[1eqy]], [[1p8z]], [[5ubo]] - hGLS +rActin<br />
**[[1yvn]] - hGLS +yActin (mutant) – yeast<br />
**[[1yvn]] - hGLS +yActin (mutant) – yeast<br />
**[[1yag]] - hGLS +yActin<br />
**[[1yag]] - hGLS +yActin<br />
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**[[3cjb]] - rGLS +rActin<br />
**[[3cjb]] - rGLS +rActin<br />
**[[3cjc]] - rGLS +rActin+DNAse I<br />
**[[3cjc]] - rGLS +rActin+DNAse I<br />
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**[[4cbu]], [[4cbw]], [[4cbx]] - mGLS +actin+Ca+ATP<br />
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**[[4cbu]], [[4cbw]], [[4cbx]], [[5mvv]] - mGLS +actin+Ca+ATP<br />
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*GLS S2
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*GLS S2 residues 178-293
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**[[5fae]], [[5faf]] - hGLS (mutant) <br />
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**[[5fae]], [[5faf]], [[5o2z]] - hGLS (mutant) <br />
**[[4s10]] - hGLS (mutant) + antibody<br />
**[[4s10]] - hGLS (mutant) + antibody<br />
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* GLS C-terminal
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* GLS domains S1-S3 residues 52-426
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 +
**[[3ffk]] – hGLS +actin <br />
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**[[1rgi]] - hoGLS +actin <br />
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* GLS domains S4-S6 residues 439-782
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 +
**[[1h1v]] - hGLS +actin + Ca + ATP<br />
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**[[2fh1]], [[2fh2]], [[2fh3]], [[2fh4]], [[1p8x]] – hGLS + Ca<br />
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**[[1nph]] - mGLS +Ca – mouse<br />
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**[[2fh1]], [[2fh2]], [[2fh3]], [[2fh4]] – hGLS <br />
 
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**[[1p8x]] - hGLS +Ca<br />
 
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**[[1p8z]] – hGLS fraction+rActin<br />
 
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:58, 29 May 2018

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

3D Structures of GLS

Updated on 29-May-2018

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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