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 Å 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.
| Original language | English |
|---|---|
| Pages (from-to) | 1447-1452 |
| Number of pages | 6 |
| Journal | Biological Chemistry |
| Volume | 383 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - Sep 1 2002 |
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Keywords
- CD81
- HCV E2 glycoprotein
- Hepatitis C virus
- Receptor protein
- Tetraspanins
ASJC Scopus subject areas
- Biochemistry
Cite this
Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop. / Kitadokoro, Kengo; Ponassi, Marco; Galli, Giuliano; Petracca, Roberto; Falugi, Fabiana; Grandi, Guido; Bolognesi, Martino.
In: Biological Chemistry, Vol. 383, No. 9, 01.09.2002, p. 1447-1452.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop
AU - Kitadokoro, Kengo
AU - Ponassi, Marco
AU - Galli, Giuliano
AU - Petracca, Roberto
AU - Falugi, Fabiana
AU - Grandi, Guido
AU - Bolognesi, Martino
PY - 2002/9/1
Y1 - 2002/9/1
N2 - 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 Å 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.
AB - 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 Å 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.
KW - CD81
KW - HCV E2 glycoprotein
KW - Hepatitis C virus
KW - Receptor protein
KW - Tetraspanins
UR - http://www.scopus.com/inward/record.url?scp=0036755086&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036755086&partnerID=8YFLogxK
U2 - 10.1515/BC.2002.164
DO - 10.1515/BC.2002.164
M3 - Article
C2 - 12437138
AN - SCOPUS:0036755086
VL - 383
SP - 1447
EP - 1452
JO - Biological Chemistry
JF - Biological Chemistry
SN - 1431-6730
IS - 9
ER -