1HNG
CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2
Summary for 1HNG
Entry DOI | 10.2210/pdb1hng/pdb |
Descriptor | CD2 (1 entity in total) |
Functional Keywords | t lymphocyte adhesion glycoprotein |
Biological source | Rattus rattus (black rat) |
Cellular location | Membrane; Single-pass type I membrane protein: P08921 |
Total number of polymer chains | 2 |
Total formula weight | 40276.04 |
Authors | Jones, E.Y.,Davis, S.J.,Williams, A.F.,Harlos, K.,Stuart, D.I. (deposition date: 1994-08-10, release date: 1995-02-07, Last modification date: 2024-10-30) |
Primary citation | Jones, E.Y.,Davis, S.J.,Williams, A.F.,Harlos, K.,Stuart, D.I. Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature, 360:232-239, 1992 Cited by PubMed Abstract: The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction. PubMed: 1279440DOI: 10.1038/360232a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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