| Structural highlights
1iv5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Related: | 1g8q |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Disease
[CD81_HUMAN] Defects in CD81 are the cause of immunodeficiency common variable type 6 (CVID6) [MIM:613496]; also called antibody deficiency due to CD81 defect. CVID6 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.[1]
Function
[CD81_HUMAN] May play an important role in the regulation of lymphoma cell growth. Interacts with a 16-kDa Leu-13 protein to form a complex possibly involved in signal transduction. May act as the viral receptor for HCV.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop.,Kitadokoro K, Ponassi M, Galli G, Petracca R, Falugi F, Grandi G, Bolognesi M Biol Chem. 2002 Sep;383(9):1447-52. PMID:12437138[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Zelm MC, Smet J, Adams B, Mascart F, Schandene L, Janssen F, Ferster A, Kuo CC, Levy S, van Dongen JJ, van der Burg M. CD81 gene defect in humans disrupts CD19 complex formation and leads to antibody deficiency. J Clin Invest. 2010 Apr;120(4):1265-74. doi: 10.1172/JCI39748. Epub 2010 Mar 8. PMID:20237408 doi:10.1172/JCI39748
- ↑ 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. 2002 Sep;383(9):1447-52. PMID:12437138
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