1lv0

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(New page: 200px<br /><applet load="1lv0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lv0, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1lv0.jpg|left|200px]]<br /><applet load="1lv0" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lv0.jpg|left|200px]]<br /><applet load="1lv0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lv0, resolution 2.00&Aring;" />
caption="1lv0, resolution 2.00&Aring;" />
'''Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide'''<br />
'''Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide'''<br />
==Overview==
==Overview==
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Rab GTPases, key regulators of membrane targeting and fusion, require the, covalent attachment of geranylgeranyl lipids to their C terminus for, function. To elucidate the role of lipid in Rab recycling, we have, determined the crystal structure of Rab guanine nucleotide dissociation, inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand, (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding, platform in a shallow hydrophobic groove. Mutation of the binding pocket, in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to, promote release of the GDI-Rab[GDP] complex from the membrane.
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Rab GTPases, key regulators of membrane targeting and fusion, require the covalent attachment of geranylgeranyl lipids to their C terminus for function. To elucidate the role of lipid in Rab recycling, we have determined the crystal structure of Rab guanine nucleotide dissociation inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding platform in a shallow hydrophobic groove. Mutation of the binding pocket in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to promote release of the GDI-Rab[GDP] complex from the membrane.
==About this Structure==
==About this Structure==
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1LV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 and GER as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LV0 OCA].
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1LV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GER:'>GER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV0 OCA].
==Reference==
==Reference==
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[[Category: Alory, C.]]
[[Category: Alory, C.]]
[[Category: An, Y.]]
[[Category: An, Y.]]
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[[Category: Balch, W.E.]]
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[[Category: Balch, W E.]]
[[Category: Chen, W.]]
[[Category: Chen, W.]]
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[[Category: Gibbs, R.A.]]
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[[Category: Gibbs, R A.]]
[[Category: Matteson, J.]]
[[Category: Matteson, J.]]
[[Category: Sakisaka, T.]]
[[Category: Sakisaka, T.]]
[[Category: Shao, Y.]]
[[Category: Shao, Y.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: GER]]
[[Category: GER]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: protein-ligand complex]]
[[Category: protein-ligand complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:54:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:43 2008''

Revision as of 11:48, 21 February 2008


1lv0, resolution 2.00Å

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Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide

Overview

Rab GTPases, key regulators of membrane targeting and fusion, require the covalent attachment of geranylgeranyl lipids to their C terminus for function. To elucidate the role of lipid in Rab recycling, we have determined the crystal structure of Rab guanine nucleotide dissociation inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding platform in a shallow hydrophobic groove. Mutation of the binding pocket in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to promote release of the GDI-Rab[GDP] complex from the membrane.

About this Structure

1LV0 is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

Geranylgeranyl switching regulates GDI-Rab GTPase recycling., An Y, Shao Y, Alory C, Matteson J, Sakisaka T, Chen W, Gibbs RA, Wilson IA, Balch WE, Structure. 2003 Mar;11(3):347-57. PMID:12623022

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