1lcj

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[[Image:1lcj.gif|left|200px]]<br /><applet load="1lcj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lcj.gif|left|200px]]
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caption="1lcj, resolution 1.8&Aring;" />
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'''SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL'''<br />
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{{Structure
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|PDB= 1lcj |SIZE=350|CAPTION= <scene name='initialview01'>1lcj</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PHS:PHOSPHONIC ACID'>PHS</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PHS:'>PHS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1LCJ OCA].
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1LCJ is a [[Protein complex]] structure of sequences 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=1LCJ OCA].
==Reference==
==Reference==
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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck., Eck MJ, Shoelson SE, Harrison SC, Nature. 1993 Mar 4;362(6415):87-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7680435 7680435]
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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck., Eck MJ, Shoelson SE, Harrison SC, Nature. 1993 Mar 4;362(6415):87-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7680435 7680435]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: complex (kinase/peptide)]]
[[Category: complex (kinase/peptide)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:17 2008''

Revision as of 10:29, 20 March 2008


PDB ID 1lcj

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL


Contents

Overview

The Src homology-2 (SH2) domains are modules of about 100 amino-acid residues that are found in many intracellular signal-transduction proteins. They bind phosphotyrosine-containing sequences with high affinity and specificity, recognizing phosphotyrosine in the context of the immediately adjacent polypeptide sequence. The protein p56lck (Lck) is a Src-like, lymphocyte-specific tyrosine kinase. A phosphopeptide library screen has recently been used to deduce an 'optimal' binding sequence for the Lck SH2 domain. There is selectivity for the residues Glu, Glu and Ile in the three positions C-terminal to the phosphotyrosine. An 11-residue phosphopeptide derived from the hamster polyoma middle-T antigen, EPQpYEEIPIYL, binds with an approximately 1 nM dissociation constant to the Lck SH2 (ref. 17), an affinity equivalent to that of the tightest known SH2-phosphopeptide complex. We report here the high-resolution crystallographic analysis of the Lck SH2 domain in complex with this phosphopeptide. Recent crystallographically derived structures of the Src SH2 domain in complex with low-affinity peptides, which do not contain the EEI consensus, and NMR-derived structures of unliganded Abl (ref. 19) and p85 (ref. 20) SH2 domains have revealed the conserved fold of the SH2 domain and the properties of a phosphotyrosine binding pocket. Our high-affinity complex shows the presence of a second pocket for the residue (pY + 3) three positions C-terminal to the phosphotyrosine (pY). The peptide is anchored by insertion of the pY and pY + 3 side chains into their pockets and by a network of hydrogen bonds to the peptide main chain. In the low-affinity phosphopeptide/Src complexes, the pY + 3 residues do not insert into the homologous binding pocket and the peptide main chain remains displaced from the surface of the domain.

Disease

Known disease associated with this structure: SCID due to LCK deficiency OMIM:[153390]

About this Structure

1LCJ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck., Eck MJ, Shoelson SE, Harrison SC, Nature. 1993 Mar 4;362(6415):87-91. PMID:7680435

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