1ees
From Proteopedia
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| - | [[Image:1ees.gif|left|200px]] | + | [[Image:1ees.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1ees |SIZE=350|CAPTION= <scene name='initialview01'>1ees</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EES is a [ | + | 1EES is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EES OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase., Gizachew D, Guo W, Chohan KK, Sutcliffe MJ, Oswald RE, Biochemistry. 2000 Apr 11;39(14):3963-71. PMID:[http:// | + | Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase., Gizachew D, Guo W, Chohan KK, Sutcliffe MJ, Oswald RE, Biochemistry. 2000 Apr 11;39(14):3963-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10747784 10747784] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:54:38 2008'' |
Revision as of 08:54, 20 March 2008
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SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES
Overview
Cdc42Hs is a member of the Ras superfamily of GTPases and initiates a cascade that begins with the activation of several kinases, including p21-activated kinase (PAK). We have previously used a 46 amino acid fragment of PAK (PBD46) to define the binding surface on Cdc42Hs [Guo et al. (1998) Biochemistry 37, 14030-14037]. Here we describe the three-dimensional solution structure of the Cdc42Hs. GMPPCP-PBD46 complex. Heteronuclear NMR methods were used to assign resonances in the complex, and approximately 2400 distance and dihedral restraints were used to calculate a set of 20 structures using a combination of distance geometry, simulated annealing, and chemical shift and Ramachandran refinement. The overall structure of Cdc42Hs in the complex differs from the uncomplexed structure in two major aspects: (1) the first alpha helix is reoriented to accommodate the binding of the peptide and (2) the regions corresponding to switch I and switch II are less disordered. As suggested by our previous work (Guo et al., 1998) and similar to the complex between Cdc42Hs and fACK [Mott et al. (1999) Nature 399, 384-388], PBD46 forms an intermolecular beta-sheet with beta2 of Cdc42Hs and contacts both switch I and switch II. The extensive binding surface between PBD46 and Cdc42Hs can account for both the high affinity of the complex and the inhibition by PBD46 of GTP hydrolysis.
About this Structure
1EES is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase., Gizachew D, Guo W, Chohan KK, Sutcliffe MJ, Oswald RE, Biochemistry. 2000 Apr 11;39(14):3963-71. PMID:10747784
Page seeded by OCA on Thu Mar 20 10:54:38 2008
