1jeg

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[[Image:1jeg.jpg|left|200px]]
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{{Structure
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|PDB= 1jeg |SIZE=350|CAPTION= <scene name='initialview01'>1jeg</scene>
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The line below this paragraph, containing "STRUCTURE_1jeg", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeg OCA], [http://www.ebi.ac.uk/pdbsum/1jeg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jeg RCSB]</span>
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'''Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP'''
'''Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP'''
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[[Category: Ji, H.]]
[[Category: Ji, H.]]
[[Category: Shekhtman, A.]]
[[Category: Shekhtman, A.]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: protein-peptide complex]]
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[[Category: Protein-peptide complex]]
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[[Category: sh3 domain]]
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[[Category: Sh3 domain]]
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[[Category: tyrosine phosphatase]]
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[[Category: Tyrosine phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:30 2008''
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Revision as of 18:07, 2 May 2008

Image:1jeg.jpg

Template:STRUCTURE 1jeg

Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP


Overview

C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells. The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain. Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP. These two residues are C-terminal to the conventional proline-rich SH3 domain recognition sequence of PEP. This interaction is required in addition to the classic polyproline helix (PPII) recognition by the Csk-SH3 domain for the association between Csk and PEP in vivo. NMR relaxation analysis suggests that Csk-SH3 has different dynamic properties in the various subsites important for peptide recognition.

About this Structure

1JEG is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

A novel, specific interaction involving the Csk SH3 domain and its natural ligand., Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D, Nat Struct Biol. 2001 Nov;8(11):998-1004. PMID:11685249 Page seeded by OCA on Fri May 2 21:07:30 2008

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