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1cxz

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|PDB= 1cxz |SIZE=350|CAPTION= <scene name='initialview01'>1cxz</scene>, resolution 2.2&Aring;
|PDB= 1cxz |SIZE=350|CAPTION= <scene name='initialview01'>1cxz</scene>, resolution 2.2&Aring;
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GSP:5&#39;-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:30:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:26:19 2008''

Revision as of 09:26, 23 March 2008

Image:1cxz.gif


PDB ID 1cxz

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1


Overview

The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 A crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, beta strands B2 and B3, and the C-terminal alpha helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.

About this Structure

1CXZ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1., Maesaki R, Ihara K, Shimizu T, Kuroda S, Kaibuchi K, Hakoshima T, Mol Cell. 1999 Nov;4(5):793-803. PMID:10619026

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