2oq1: Difference between revisions

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|PDB= 2oq1 |SIZE=350|CAPTION= <scene name='initialview01'>2oq1</scene>, resolution 1.9&Aring;
|PDB= 2oq1 |SIZE=350|CAPTION= <scene name='initialview01'>2oq1</scene>, resolution 1.9&Aring;
|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.
==Disease==
Known diseases associated with this structure: Immunodeficiency due to defect in CD3-zeta OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186780 186780]], Selective T-cell defect OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176947 176947]]


==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: PB]]
[[Category: tandem sh2 domain]]
[[Category: tandem sh2 domain]]
[[Category: tyrosine kinase]]
[[Category: tyrosine kinase]]
[[Category: zap-70]]
[[Category: zap-70]]


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Revision as of 04:21, 31 March 2008

File:2oq1.gif


PDB ID 2oq1

Drag the structure with the mouse to rotate
, resolution 1.9Å
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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