1ukv

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(New page: 200px<br /><applet load="1ukv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ukv, resolution 1.50&Aring;" /> '''Structure of RabGDP-...)
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[[Image:1ukv.gif|left|200px]]<br /><applet load="1ukv" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ukv.gif|left|200px]]<br /><applet load="1ukv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ukv, resolution 1.50&Aring;" />
caption="1ukv, resolution 1.50&Aring;" />
'''Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase'''<br />
'''Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase'''<br />
==Overview==
==Overview==
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Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key, membrane traffic regulators in eukaryotic cells whose function is governed, by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using, a combination of chemical synthesis and protein engineering, we generated, and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of, the complex was solved to 1.5 angstrom resolution and provides a, structural basis for the ability of RabGDI to inhibit the release of, nucleotide by Rab proteins. Isoprenoid binding requires a conformational, change that opens a cavity in the hydrophobic core of its domain II., Analysis of the structure provides a molecular basis for understanding a, RabGDI mutant that causes mental retardation in humans.
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Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.
==About this Structure==
==About this Structure==
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1UKV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, GER and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKV OCA].
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1UKV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GER:'>GER</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKV OCA].
==Reference==
==Reference==
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[[Category: Brunsveld, L.]]
[[Category: Brunsveld, L.]]
[[Category: Durek, T.]]
[[Category: Durek, T.]]
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[[Category: Goody, R.S.]]
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[[Category: Goody, R S.]]
[[Category: Kushnir, S.]]
[[Category: Kushnir, S.]]
[[Category: Pylypenko, O.]]
[[Category: Pylypenko, O.]]
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[[Category: vesicular transport]]
[[Category: vesicular transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:12:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:37 2008''

Revision as of 13:25, 21 February 2008


1ukv, resolution 1.50Å

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Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

Overview

Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.

About this Structure

1UKV is a Protein complex structure of sequences from Saccharomyces cerevisiae with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase., Rak A, Pylypenko O, Durek T, Watzke A, Kushnir S, Brunsveld L, Waldmann H, Goody RS, Alexandrov K, Science. 2003 Oct 24;302(5645):646-50. PMID:14576435

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