1ab2: Difference between revisions

Revision as of 10:03, 2 May 2008

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL

OverviewOverview

SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine. The solution structure of the abl SH2 product, a protein of 109 residues and 12.1 kd, has been determined by multidimensional nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a pair of three-stranded antiparallel beta sheets and a C-terminal alpha helix enclosing the hydrophobic core. Three arginines project from a short N-terminal alpha helix and one beta sheet into the putative phosphotyrosine-binding site, which lies on a face distal from the termini. Comparison with other SH2 sequences supports a common global fold and mode of phosphotyrosine binding for this family.

About this StructureAbout this Structure

1AB2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional solution structure of the src homology 2 domain of c-abl., Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D, Cell. 1992 Aug 21;70(4):697-704. PMID:1505033 Page seeded by OCA on Fri May 2 10:03:43 2008

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OCA

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 [[Image:1ab2.gif|left|200px]]
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-}}
 '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL'''
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 [[Category: Overduin, M.]]
 [[Category: Rios, C B.]]
-[[Category: transferase(phosphotransferase)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:03:43 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:36:53 2008''