1ksw: Difference between revisions

Revision as of 10:55, 2 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:1ksw.png

Template:STRUCTURE 1ksw

Structure of Human c-Src Tyrosine Kinase (Thr338Gly Mutant) in Complex with N6-benzyl ADPStructure of Human c-Src Tyrosine Kinase (Thr338Gly Mutant) in Complex with N6-benzyl ADP

Template:ABSTRACT PUBMED 11841936

About this StructureAbout this Structure

1KSW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Mutant tyrosine kinases with unnatural nucleotide specificity retain the structure and phospho-acceptor specificity of the wild-type enzyme., Witucki LA, Huang X, Shah K, Liu Y, Kyin S, Eck MJ, Shokat KM, Chem Biol. 2002 Jan;9(1):25-33. PMID:11841936

Page seeded by OCA on Wed Jul 2 10:55:46 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ksw.gif|left|200px]]
+{{Seed}}
+[[Image:1ksw.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ksw|  PDB=1ksw  |  SCENE=  }}
-'''Structure of Human c-Src Tyrosine Kinase (Thr338Gly Mutant) in Complex with N6-benzyl ADP'''
+===Structure of Human c-Src Tyrosine Kinase (Thr338Gly Mutant) in Complex with N6-benzyl ADP===
-==Overview==
+<!--
-The direct substrates of one protein kinase in a cell can be identified by mutation of the ATP binding pocket to allow an unnatural ATP analog to be accepted exclusively by the engineered kinase. Here, we present structural and functional assessment of peptide specificity of mutant protein kinases with unnatural ATP analogs. The crystal structure (2.8 A resolution) of c-Src (T338G) with N(6)-(benzyl) ADP bound shows that the creation of a unique nucleotide binding pocket does not alter the phospho-acceptor binding site of the kinase. A panel of optimal peptide substrates of defined sequence, as well as a degenerate peptide library, was utilized to assess the phospho-acceptor specificity of the engineered "traceable" kinases. The specificity profiles for the mutant kinases were found to be identical to those of their wild-type counterparts.
+The line below this paragraph, {{ABSTRACT_PUBMED_11841936}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11841936 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11841936}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Sh2]]
 [[Category: Sh3]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:08:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:55:46 2008''