[Spatial structure of a Fab-fragment of a monoclonal antibody to human interleukin-2 in two crystalline forms at a resolution of 2.2 and 2.9 angstroms].
The three-dimensional structure of the antigen-binding fragment of a monoclonal antibody to human interleukin-2 was determined in two crystal forms by the X-ray method of molecular replacement at 2.2 and 2.9 A resolutions. The spatial structure of the protein and the stereochemistry of its antigen-binding site were analyzed.
Fokin
A V
AV
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Afonin
P V
PV
Mikhaĭlova
I Iu
IIu
Tsygannik
I N
IN
Mareeva
T Iu
TIu
Nesmeianov
V A
VA
Pangborn
W
W
Lee
N
N
Duax
W
W
Siszak
E
E
Pletnev
V Z
VZ
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000276:immunology; D000941:Antigens / Q000276:immunology; D001666:Binding Sites, Antibody; D018360:Crystallography, X-Ray; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000276:immunology; D007376:Interleukin-2 / Q000276:immunology*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013237:Stereoisomerism
D000911:Antibodies, Monoclonal; D000941:Antigens; D007140:Immunoglobulin Fab Fragments; D007376:Interleukin-2