A binding site for the T-cell co-receptor CD8 on the α3 domain of HLA-A2

Adhesion measurements between CD8 and 48 point mutants of HLA-A2.1 show that the CD8 α-chain binds to the α 3 domain of HLA-A2.1. Three clusters of α 3 residues contribute to the binding, with an exposed, negatively charged loop (residues 223–229) playing a dominant role. CD8 binding correlates with...

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Veröffentlicht in:	Nature (London) 1990-05, Vol.345 (6270), p.41-46
Hauptverfasser:	Salter, Russell D., Benjamin, Richard J., Wesley, Pamela K., Buxton, Sarah E., Garrett, Thomas P. J., Clayberger, Carol, Krensky, Alan M., Norment, Anne M., Littman, Dan R., Parham, Peter
Format:	Artikel
Sprache:	eng
Schlagworte:	Adhesion tests Antibodies Antigens Binding sites CD8 antigen Cell activation Cell adhesion & migration Cell recognition Cytotoxicity Histocompatibility antigen HLA Humanities and Social Sciences Immunoglobulins Kinases Lymphocytes Lymphocytes T Major histocompatibility complex multidisciplinary Mutation Peptides Recognition Residues Science Science (multidisciplinary) T cell receptors
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