2oq1: Difference between revisions
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'''Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide''' | '''Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide''' | ||
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[[Category: Morgenstern, J.]] | [[Category: Morgenstern, J.]] | ||
[[Category: Ram, M K.]] | [[Category: Ram, M K.]] | ||
[[Category: | [[Category: Tandem sh2 domain]] | ||
[[Category: | [[Category: Tyrosine kinase]] | ||
[[Category: | [[Category: Zap-70]] | ||
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Revision as of 11:25, 4 May 2008
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 Page seeded by OCA on Sun May 4 11:25:31 2008