2OQ1

Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide

Summary for 2OQ1

• Entry DOI: 10.2210/pdb2oq1/pdb
• Descriptor: Tyrosine-protein kinase ZAP-70, T-cell surface glycoprotein CD3 zeta chain, LEAD (II) ION, ... (4 entities in total)
• Functional Keywords: tandem sh2 domains, zap-70, tyrosine kinase, transferase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 31629.33

Authors

Hatada, M.H.,Laird, E.R.,Green, J.,Morgenstern, J.,Ram, M.K. (deposition date: 2007-01-30, release date: 2007-03-06, Last modification date: 2024-11-06)

Primary citation

Hatada, M.H.,Lu, X.,Laird, E.R.,Green, J.,Morgenstern, J.P.,Lou, M.,Marr, C.,Phillips, T.B.,Ram, M.K.,Theriault, K.
Molecular basis for the interaction of ZAP-70 with the T-cell receptor
Nature, 377:32-38, 1995

PubMed Abstract: 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.

PubMed: 7659156
DOI: 10.1038/377032a0

Experimental method

X-RAY DIFFRACTION (1.9 Å)