Wang J H, Yan Y W, Garrett T P, Liu J H, Rodgers D W, Garlick R L, Tarr G E, Husain Y, Reinherz E L, Harrison S C
Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, Massachusetts.
Nature. 1990 Nov 29;348(6300):411-8. doi: 10.1038/348411a0.
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.
已确定CD4的N端片段结构的分辨率为2.4埃。它有两个紧密邻接的结构域,由一条连续的β链连接。两者都具有免疫球蛋白折叠,但结构域2有一个截短的β桶和一个非标准二硫键。单克隆抗体、II类主要组织相容性复合体分子和人类免疫缺陷病毒gp120的结合位点可定位在分子表面。