Subunit Association and Conformational Flexibility in the Head Subdomain of Human CD81 Large Extracellular Loop : Biological Chemistry Jump to ContentJump to Main Navigation
Show Summary Details

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

249,00 € / $374.00 / £187.00*

Online
ISSN
1437-4315
See all formats and pricing

 


 
 

Select Volume and Issue
Loading journal volume and issue information...

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

K. Kitadokoro / M. Ponassi / G. Galli / R. Petracca / F. Falugi / G. Grandi / M. Bolognesi

Citation Information: Biological Chemistry. Volume 383, Issue 9, Pages 1447–1452, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2002.164, June 2005

Publication History

Published Online:
2005-06-01

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 threedimensional structure, solved and refined at 2.6 å resolution (Rfactor = 22.8%), shows that the protein adopts a dimeric assembly, based on an association interface built up by tetraspaninconserved 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.

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Yahya Homsi, Jan-Gero Schloetel, Konstanze D. Scheffer, Thomas H. Schmidt, Nicolas Destainville, Luise Florin, and Thorsten Lang
Biophysical Journal, 2014, Volume 107, Number 1, Page 100
[2]
L. Kong, E. Giang, T. Nieusma, R. U. Kadam, K. E. Cogburn, Y. Hua, X. Dai, R. L. Stanfield, D. R. Burton, A. B. Ward, I. A. Wilson, and M. Law
Science, 2013, Volume 342, Number 6162, Page 1090
[3]
Dibyendu Chakraborty, Karla K. Rodgers, Shannon M. Conley, and Muna I. Naash
FEBS Journal, 2013, Volume 280, Number 1, Page 127
[4]
Shannon M. Conley, Michael W. Stuck, and Muna I. Naash
Cellular and Molecular Life Sciences, 2012, Volume 69, Number 7, Page 1035
[5]
Hideki Nakajima, Laurence Cocquerel, Nobutaka Kiyokawa, Junichiro Fujimoto, and Shoshana Levy
Biochemical and Biophysical Research Communications, 2005, Volume 328, Number 4, Page 1091
[6]
Alexander Neugebauer, Christian D.P. Klein, and Rolf W. Hartmann
Bioorganic & Medicinal Chemistry Letters, 2004, Volume 14, Number 7, Page 1765
[7]
Martin E. Hemler
Annual Review of Cell and Developmental Biology, 2003, Volume 19, Number 1, Page 397
[8]
Shoshana Levy and Tsipi Shoham
Nature Reviews Immunology, 2005, Volume 5, Number 2, Page 136
[9]
T. Schäfer, P. Starkl, C. Allard, R. M. Wolf, and T. Schweighoffer
Allergy, 2010, Volume 65, Number 10, Page 1242
[10]
Shoshana Levy
AfCS-Nature Molecule Pages, 2010
[11]
B Wang, F Li, J Xiang, L Gui, Z Luo, and H Yan
Journal of Fish Diseases, 2010, Volume 33, Number 1, Page 15
[12]
Marcel Holzer, Sigrid Ziegler, Alexander Neugebauer, Bernd Kronenberger, Christian D. Klein, and Rolf W. Hartmann
Archiv der Pharmazie, 2008, Volume 341, Number 8, Page 478
[13]
Kengo Kitadokoro
Uirusu, 2004, Volume 54, Number 1, Page 39

Comments (0)

Please log in or register to comment.