| Autor: |
Wang JH; Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, Massachusetts., Yan YW, Garrett TP, Liu JH, Rodgers DW, Garlick RL, Tarr GE, Husain Y, Reinherz EL, Harrison SC |
| Jazyk: |
angličtina |
| Zdroj: |
Nature [Nature] 1990 Nov 29; Vol. 348 (6300), pp. 411-8. |
| DOI: |
10.1038/348411a0 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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