Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution.
A secreted fragment of the extracellular portion of human CD8 alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 A resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8 alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.
Leahy
D J
DJ
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Axel
R
R
Hendrickson
W A
WA
D000595:Amino Acid Sequence; D000818:Animals; D016827:CD8 Antigens / Q000737:chemistry* / Q000302:isolation & purification; D016466:CHO Cells / Q000378:metabolism; D006224:Cricetinae; D003461:Crystallography; D015870:Gene Expression; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D016415:Sequence Alignment
D016827:CD8 Antigens