This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1g8q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8q OCA], [http://www.ebi.ac.uk/pdbsum/1g8q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g8q RCSB]</span>
}}
}}
Line 31: Line 34:
[[Category: alpha helical]]
[[Category: alpha helical]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:47 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:38:57 2008''

Revision as of 17:38, 30 March 2008


PDB ID 1g8q

Drag the structure with the mouse to rotate
, resolution 1.60Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN CD81 EXTRACELLULAR DOMAIN, A RECEPTOR FOR HEPATITIS C VIRUS


Overview

Human CD81, a known receptor for hepatitis C virus envelope E2 glycoprotein, is a transmembrane protein belonging to the tetraspanin family. The crystal structure of human CD81 large extracellular domain is reported here at 1.6 A resolution. Each subunit within the homodimeric protein displays a mushroom-like structure, composed of five alpha-helices arranged in 'stalk' and 'head' subdomains. Residues known to be involved in virus binding can be mapped onto the head subdomain, providing a basis for the design of antiviral drugs and vaccines. Sequence analysis of 160 tetraspanins indicates that key structural features and the new protein fold observed in the CD81 large extracellular domain are conserved within the family. On these bases, it is proposed that tetraspanins may assemble at the cell surface into homo- and/or hetero-dimers through a conserved hydrophobic interface located in the stalk subdomain, while interacting with other liganding proteins, including hepatitis C virus E2, through the head subdomain. The topology of such interactions provides a rationale for the assembly of the so-called tetraspan-web.

About this Structure

1G8Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs., Kitadokoro K, Bordo D, Galli G, Petracca R, Falugi F, Abrignani S, Grandi G, Bolognesi M, EMBO J. 2001 Jan 15;20(1-2):12-8. PMID:11226150

Page seeded by OCA on Sun Mar 30 20:38:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools