2oq1: Difference between revisions
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|PDB= 2oq1 |SIZE=350|CAPTION= <scene name='initialview01'>2oq1</scene>, resolution 1.9Å | |PDB= 2oq1 |SIZE=350|CAPTION= <scene name='initialview01'>2oq1</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene> | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oq1 OCA], [http://www.ebi.ac.uk/pdbsum/2oq1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oq1 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the zeta-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of alpha-helices connects the two SH2 domains, producing an interface that constitutes one of the two critical phosphotyrosine binding sites. These and other unique features provide the molecular basis for highly selective association of ZAP-70 with the T-cell receptor. | The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the zeta-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of alpha-helices connects the two SH2 domains, producing an interface that constitutes one of the two critical phosphotyrosine binding sites. These and other unique features provide the molecular basis for highly selective association of ZAP-70 with the T-cell receptor. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Morgenstern, J.]] | [[Category: Morgenstern, J.]] | ||
[[Category: Ram, M K.]] | [[Category: Ram, M K.]] | ||
[[Category: tandem sh2 domain]] | [[Category: tandem sh2 domain]] | ||
[[Category: tyrosine kinase]] | [[Category: tyrosine kinase]] | ||
[[Category: zap-70]] | [[Category: zap-70]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:21:27 2008'' |
Revision as of 04:21, 31 March 2008
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, resolution 1.9Å | |||||||
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Ligands: | , , | ||||||
Activity: | Non-specific protein-tyrosine kinase, with EC number 2.7.10.2 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide
OverviewOverview
The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the zeta-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of alpha-helices connects the two SH2 domains, producing an interface that constitutes one of the two critical phosphotyrosine binding sites. These and other unique features provide the molecular basis for highly selective association of ZAP-70 with the T-cell receptor.
About this StructureAbout this Structure
2OQ1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor., Hatada MH, Lu X, Laird ER, Green J, Morgenstern JP, Lou M, Marr CS, Phillips TB, Ram MK, Theriault K, et al., Nature. 1995 Sep 7;377(6544):32-8. PMID:7659156
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