1ees: Difference between revisions

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[[Image:1ees.gif|left|200px]]<br />

[[Image:1ees.gif|left|200px]]<br /><applet load="1ees" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1ees" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ees" />

'''SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Protein_complex 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EES OCA].

1EES is a [http://en.wikipedia.org/wiki/Protein_complex 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==

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Line 14:

[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Chohan, K.C.]]

[[Category: Chohan, K C.]]

[[Category: Gizachew, D.]]

[[Category: Guo, W.]]

[[Category: Oswald, R.E.]]

[[Category: Oswald, R E.]]

[[Category: Sutcliffe, M.J.]]

[[Category: Sutcliffe, M J.]]

[[Category: protein-protein complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:42:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:57 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ees.gif|left|200px]]<br />
+[[Image:1ees.gif|left|200px]]<br /><applet load="1ees" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ees" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ees" />
 '''SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES'''<br />
 ==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.
+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==
-EES is a [http://en.wikipedia.org/wiki/Protein_complex 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EES OCA].
+EES is a [http://en.wikipedia.org/wiki/Protein_complex 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==
@@ Line 15: / Line 14: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Chohan, K.C.]]
+[[Category: Chohan, K C.]]
 [[Category: Gizachew, D.]]
 [[Category: Guo, W.]]
-[[Category: Oswald, R.E.]]
+[[Category: Oswald, R E.]]
-[[Category: Sutcliffe, M.J.]]
+[[Category: Sutcliffe, M J.]]
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:42:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:57 2008''