1IV5

New Crystal Form of Human CD81 Large Extracellular Loop.

Summary for 1IV5

• Entry DOI: 10.2210/pdb1iv5/pdb
• Related: 1G8Q
• Descriptor: CD81 antigen (2 entities in total)
• Functional Keywords: alpha domain, five helix, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Multi-pass membrane protein: P60033
• Total number of polymer chains: 2
• Total formula weight: 19834.15

Authors

Kitadokoro, K.,Bolognesi, M.,Grandi, G.,Marco, P.,Galli, G.,Petracca, R.,Fabiana, F. (deposition date: 2002-03-14, release date: 2003-01-28, Last modification date: 2024-10-16)

Primary citation

Kitadokoro, K.,Ponassi, M.,Galli, G.,Petracca, R.,Falugi, F.,Grandi, G.,Bolognesi, M.
Subunit Association and Conformational Flexibility in the Head-subdomain of Human CD81 Large Extracellular Loop.
Biol.Chem., 383:1447-1452, 2002

PubMed Abstract: 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.

PubMed: 12437138
DOI: 10.1515/BC.2002.164

Experimental method

X-RAY DIFFRACTION (2.6 Å)