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1doa

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(New page: 200px<br /> <applet load="1doa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1doa, resolution 2.60&Aring;" /> '''STRUCTURE OF THE RH...)
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<applet load="1doa" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1doa, resolution 2.60&Aring;" />
'''STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI'''<br />
'''STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI'''<br />
==Overview==
==Overview==
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The RhoGDI proteins serve as key multifunctional regulators of Rho family, GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the, Cdc42/RhoGDI complex reveals two important sites of interaction between, GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds, to the switch I and II domains of Cdc42 leading to the inhibition of both, GDP dissociation and GTP hydrolysis. Second, the geranylgeranyl moiety of, Cdc42 inserts into a hydrophobic pocket within the immunoglobulin-like, domain of the GDI molecule leading to membrane release. The structural, data demonstrate how GDIs serve as negative regulators of small, GTP-binding proteins and how the isoprenoid moiety is utilized in this, critical regulatory interaction.
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The RhoGDI proteins serve as key multifunctional regulators of Rho family GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the Cdc42/RhoGDI complex reveals two important sites of interaction between GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the inhibition of both GDP dissociation and GTP hydrolysis. Second, the geranylgeranyl moiety of Cdc42 inserts into a hydrophobic pocket within the immunoglobulin-like domain of the GDI molecule leading to membrane release. The structural data demonstrate how GDIs serve as negative regulators of small GTP-binding proteins and how the isoprenoid moiety is utilized in this critical regulatory interaction.
==About this Structure==
==About this Structure==
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1DOA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, GDP 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=1DOA OCA].
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1DOA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GDP:'>GDP</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=1DOA OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Cerione, R.C.]]
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[[Category: Cerione, R C.]]
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[[Category: Hoffman, G.R.]]
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[[Category: Hoffman, G R.]]
[[Category: Nassar, N.]]
[[Category: Nassar, N.]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: x-ray]]
[[Category: x-ray]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:34:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:40 2008''

Revision as of 10:18, 21 February 2008


1doa, resolution 2.60Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI

Overview

The RhoGDI proteins serve as key multifunctional regulators of Rho family GTP-binding proteins. The 2.6 A X-ray crystallographic structure of the Cdc42/RhoGDI complex reveals two important sites of interaction between GDI and Cdc42. First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the inhibition of both GDP dissociation and GTP hydrolysis. Second, the geranylgeranyl moiety of Cdc42 inserts into a hydrophobic pocket within the immunoglobulin-like domain of the GDI molecule leading to membrane release. The structural data demonstrate how GDIs serve as negative regulators of small GTP-binding proteins and how the isoprenoid moiety is utilized in this critical regulatory interaction.

About this Structure

1DOA is a Protein complex structure of sequences from Bos taurus and Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI., Hoffman GR, Nassar N, Cerione RA, Cell. 2000 Feb 4;100(3):345-56. PMID:10676816

Page seeded by OCA on Thu Feb 21 12:18:40 2008

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