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.
Wang
J H
JH
Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, Massachusetts.
Yan
Y W
YW
Garrett
T P
TP
Liu
J H
JH
Rodgers
D W
DW
Garlick
R L
RL
Tarr
G E
GE
Husain
Y
Y
Reinherz
E L
EL
Harrison
S C
SC
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