Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains

The structure of an N-terminal fragment of CD4 has been determined to 2.4 A resolution. It has two tightly abutting domains connected by a continuous beta strand. Both have the immunoglobulin fold, but domain 2 has a truncated beta barrel and a non-standard disulphide bond. The binding sites for mon...

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Veröffentlicht in:Nature (London) 1990-11, Vol.348 (6300), p.411-418
Hauptverfasser: Wang, Jiahuai, Yan, Youwei, Garrett, Thomas P. J, Liu, Jinhuan, Rodgers, David W, Garlick, Robert L, Tarr, George E, Husain, Yasmin, Reinherz, Ellis L, Harrison, Stephen C
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Sprache:eng
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Zusammenfassung:The structure of an N-terminal fragment of CD4 has been determined to 2.4 A resolution. It has two tightly abutting domains connected by a continuous beta strand. Both have the immunoglobulin fold, but domain 2 has a truncated beta barrel and a non-standard disulphide bond. The binding sites for monoclonal antibodies, class II major histocompatibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
ISSN:0028-0836
1476-4687
DOI:10.1038/348411a0