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 monoclonal antibodies, class II major histocompatibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, Massachusetts.
J H
JH
Wang
Y W
YW
Yan
T P
TP
Garrett
J H
JH
Liu
D W
DW
Rodgers
R L
RL
Garlick
G E
GE
Tarr
Y
Y
Husain
E L
EL
Reinherz
S C
SC
Harrison
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D001665:Binding Sites; D015704:CD4 Antigens / Q000276:immunology / Q000648:ultrastructure*; D003461:Crystallography; D000939:Epitopes; D015699:HIV Envelope Protein gp120 / Q000378:metabolism; D006681:HLA-D Antigens / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D000911:Antibodies, Monoclonal; D015704:CD4 Antigens; D000939:Epitopes; D015699:HIV Envelope Protein gp120; D006681:HLA-D Antigens; D010446:Peptide Fragments; D011994:Recombinant Proteins