1CDB

STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2

Summary for 1CDB

• Entry DOI: 10.2210/pdb1cdb/pdb
• Descriptor: CD2 (1 entity in total)
• Functional Keywords: t lymphocyte adhesion glycoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P06729
• Total number of polymer chains: 1
• Total formula weight: 12453.22

Authors

Wyss, D.F.,Withka, J.M.,Recny, M.A.,Wagner, G. (deposition date: 1993-09-15, release date: 1994-01-31, Last modification date: 2024-05-22)

Primary citation

Withka, J.M.,Wyss, D.F.,Wagner, G.,Arulanandam, A.R.,Reinherz, E.L.,Recny, M.A.
Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2.
Structure, 1:69-81, 1993

PubMed Abstract: CD2, a T-cell specific surface glycoprotein, is critically important for mediating adherence of T cells to antigen-presenting cells or target cells. Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3) expressed on the cell to which the T cell binds. Human CD2 domain 1 requires N-linked carbohydrate to maintain its native conformation and ability to bind CD58. In contrast, rat CD2 does not require N-linked carbohydrate, and binds to a different ligand, CD48.

PubMed: 7915183
DOI: 10.1016/0969-2126(93)90009-6

Experimental method

SOLUTION NMR