2ase: Difference between revisions

Revision as of 11:16, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ase.png

Template:STRUCTURE 2ase

NMR structure of the F28L mutant of Cdc42HsNMR structure of the F28L mutant of Cdc42Hs

Template:ABSTRACT PUBMED 16489751

About this StructureAbout this Structure

2ASE is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure of an oncogenic mutant of Cdc42Hs., Adams PD, Oswald RE, Biochemistry. 2006 Feb 28;45(8):2577-83. PMID:16489751

Page seeded by OCA on Tue Jul 29 11:16:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ase.gif|left|200px]]
+{{Seed}}
+[[Image:2ase.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2ase|  PDB=2ase  |  SCENE=  }}
-'''NMR structure of the F28L mutant of Cdc42Hs'''
+===NMR structure of the F28L mutant of Cdc42Hs===
-==Overview==
+<!--
-Cdc42Hs(F28L) is a single-point mutant of Cdc42Hs, a member of the Ras superfamily of GTP-binding proteins, that facilitates cellular transformation brought about by an increased rate of cycling between GTP and GDP [Lin, R., et al. (1997) Curr. Biol. 7, 794-797]. Dynamics studies of Cdc42Hs(F28L)-GDP have shown increased flexibility for several residues at the nucleotide-binding site [Adams, P. D., et al. (2004) Biochemistry 43, 9968-9977]. The solution structure of Cdc42Hs-GDP (wild type) has previously been determined by NMR spectroscopy [Feltham, J. L., et al. (1997) Biochemistry 36, 8755-8766]. Here, we describe the solution structure of Cdc42Hs(F28L)-GDP, which provides insight into the structural basis for the change in affinity for GDP. Heteronuclear NMR experiments were performed to assign resonances in the protein, and distance, hydrogen bonding, residual dipolar coupling, and dihedral angle constraints were used to calculate a set of low-energy structures using distance geometry and simulated annealing refinement protocols. The overall structure of Cdc42Hs(F28L)-GDP is very similar to that of wild-type Cdc42Hs, consisting of a centrally located six-stranded beta-sheet structure surrounding the C-terminal alpha-helix [Feltham, J. L., et al. (1997) Biochemistry 36, 8755-8766]. In addition, the same three regions in wild-type Cdc42Hs that show structural disorder (Switch I, Switch II, and the Insert region) are disordered in F28L as well. Although the structure of Cdc42Hs(F28L)-GDP is very similar to that of the wild type, interactions with the nucleotide and hydrogen bonding within the nucleotide binding site are altered, and the region surrounding L28 is substantially more disordered.
+The line below this paragraph, {{ABSTRACT_PUBMED_16489751}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16489751 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16489751}}
 ==About this Structure==
-ASE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASE OCA].
+ASE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASE OCA].
 ==Reference==
@@ Line 27: / Line 31: @@
 [[Category: G-protein]]
 [[Category: Gtp binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:25:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:16:07 2008''