Summary
PDB 1IV5 deposited: 2002-03-14 modified: 2009-02-24
Title New Crystal Form of Human CD81 Large Extracellular Loop.
Authors Bolognesi, M., Falugi, F., Galli, G., Grandi, G., Kitadokoro, K., Petracca, R., Ponassi, M.
Method X-RAY DIFFRACTION
Structure factors resolution 2.6 rfactor 0.2287 rfree 0.2822
DPI 1.09 theoretical min: 0.44
Citations

The large extracellular loop of human CD81, a tetraspanin mediating hepatitis C virus envelope protein E2 binding to human cells, has been crystallized in a hexagonal form. The three-dimensional structure, solved and refined at 2.6 A resolution (R-factor = 22.8%), shows that the protein adopts a dimeric assembly, based on an association interface built up by tetraspanin-conserved residues. Structural comparisons with the tertiary structure of human CD81 large extracellular loop, previously determined in a different crystal form, show marked conformational fluctuations in the molecular regions thought to be involved in binding to the viral protein, suggesting rules for recognition and assembly within the tetraspan web.

Biol.Chem. 2002 Sep; 383(9):1447-1452 doi:10.1515/BC.2002.164

Cross References
Database source Identifier Description
PubMed 12437138
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1IV5/1 1IV5 1 dimer 0 2 0 1295