Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-09

AUTHORS

Marcos H. Hatada, Xiaode Lu, Ellen R. Laird, Jeremy Green, Jay P. Morgenstern, Meizhen Lou, Chris S. Marr, Thomas B. Phillips, Mary K. Ram, Kelly Theriault, Mark J. Zoller, Jennifer L. Karas

ABSTRACT

The crystal structure of the tandem SH2 domains of human ZAP-70 in complex with a peptide derived from the ζ-subunit of the T-cell receptor reveals an unanticipated interaction between the two domains. A coiled coil of α-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. More... »

PAGES

32-38

Journal

TITLE

Nature

ISSUE

6544

VOLUME

377

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/377032a0

DOI

http://dx.doi.org/10.1038/377032a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001223281

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7659156


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