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The large extracellular loop of human CD81, atetraspanin mediating hepatitis C virus envelope protein E2 binding to humancells, has been crystallized in a hexagonal form. The threedimensionalstructure, solved and refined at 2.6 å resolution (Rfactor = 22.8%), shows thatthe protein adopts a dimeric assembly, based on an association interface builtup by tetraspaninconserved residues. Structural comparisons with the tertiarystructure of human CD81 large extracellular loop, previously determined in adifferent crystal form, show marked conformational fluctuations in themolecular regions thought to be involved in binding to the viral protein,suggesting rules for recognition and assembly within the tetraspan web.

Subunit Association and Conformational Flexibility in the Head Subdomain of Human CD81 Large Extracellular Loop