1jeg
From Proteopedia
(New page: 200px<br /><applet load="1jeg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jeg" /> '''Solution structure of the SH3 domain from C-...) |
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| - | [[Image:1jeg.jpg|left|200px]]<br /><applet load="1jeg" size=" | + | [[Image:1jeg.jpg|left|200px]]<br /><applet load="1jeg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jeg" /> | caption="1jeg" /> | ||
'''Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP'''<br /> | '''Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | C-terminal Src kinase (Csk) takes part in a highly specific, high affinity | + | 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== | ==About this Structure== | ||
| - | 1JEG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http:// | + | 1JEG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cowburn, D.]] | [[Category: Cowburn, D.]] | ||
[[Category: Ghose, R.]] | [[Category: Ghose, R.]] | ||
| - | [[Category: Goger, M | + | [[Category: Goger, M J.]] |
[[Category: Ji, H.]] | [[Category: Ji, H.]] | ||
[[Category: Shekhtman, A.]] | [[Category: Shekhtman, A.]] | ||
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[[Category: tyrosine phosphatase]] | [[Category: tyrosine phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:44 2008'' |
Revision as of 11:21, 21 February 2008
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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. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 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
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