1HNF
CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION
Summary for 1HNF
Entry DOI | 10.2210/pdb1hnf/pdb |
Descriptor | CD2, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION, ... (4 entities in total) |
Functional Keywords | t lymphocyte adhesion glycoprotein |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 21688.69 |
Authors | Bodian, D.L.,Jones, E.Y.,Harlos, K.,Stuart, D.I.,Davis, S.J. (deposition date: 1994-08-10, release date: 1995-02-07, Last modification date: 2024-10-16) |
Primary citation | Bodian, D.L.,Jones, E.Y.,Harlos, K.,Stuart, D.I.,Davis, S.J. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution. Structure, 2:755-766, 1994 Cited by PubMed Abstract: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo. The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands. Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition. PubMed: 7994575DOI: 10.1016/S0969-2126(94)00076-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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