1CD8

CRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T CELL CO-RECEPTOR CD8 AT 2.6 ANGSTROMS RESOLUTION

Summary for 1CD8

• Entry DOI: 10.2210/pdb1cd8/pdb
• Descriptor: T CELL CORECEPTOR CD8, SULFATE ION (3 entities in total)
• Functional Keywords: surface glycoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P01732
• Total number of polymer chains: 1
• Total formula weight: 12945.61

Authors

Leahy, D.J.,Axel, R.,Hendrickson, W.A. (deposition date: 1992-01-16, release date: 1994-01-31, Last modification date: 2024-10-30)

Primary citation

Leahy, D.J.,Axel, R.,Hendrickson, W.A.
Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution.
Cell(Cambridge,Mass.), 68:1145-1162, 1992

PubMed Abstract: 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.

PubMed: 1547508
DOI: 10.1016/0092-8674(92)90085-Q

Experimental method

X-RAY DIFFRACTION (2.6 Å)