We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1eaj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eaj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1eaj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eaj| PDB=1eaj | SCENE= }}
{{STRUCTURE_1eaj| PDB=1eaj | SCENE= }}
-
'''DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN AT 1.35 ANGSTROM RESOLUTION'''
+
===DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN AT 1.35 ANGSTROM RESOLUTION===
-
==Overview==
+
<!--
-
BACKGROUND: The coxsackievirus and adenovirus receptor (CAR) comprises two extracellular immunoglobulin domains, a transmembrane helix and a C-terminal intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is necessary and sufficient for adenovirus binding, whereas the site of coxsackievirus attachment has not yet been localized. The normal cellular role of CAR is currently unknown, although CAR was recently proposed to function as a homophilic cell adhesion molecule. RESULTS: The human CAR D1 domain was bacterially expressed and crystallized. The structure was solved by molecular replacement using the structure of CAR D1 bound to the adenovirus type 12 fiber head and refined to 1.7 A resolution, including individual anisotropic temperature factors. The two CAR D1 structures are virtually identical, apart from the BC, C"D, and FG loops that are involved both in fiber head binding and homodimerization in the crystal. Analytical equilibrium ultracentrifugation shows that a dimer also exists in solution, with a dissociation constant of 16 microM. CONCLUSIONS: The CAR D1 domain forms homodimers in the crystal using the same GFCC'C" surface that interacts with the adenovirus fiber head. The homodimer is very similar to the CD2 D1-CD58 D1 heterodimer. CAR D1 also forms dimers in solution with a dissociation constant typical of other cell adhesion complexes. These results are consistent with reports that CAR may function physiologically as a homophilic cell adhesion molecule in the developing mouse brain. Adenovirus may thus have recruited an existing and conserved interaction surface of CAR to use for its own cell attachment.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11080637}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11080637 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11080637}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Symmetric dimer]]
[[Category: Symmetric dimer]]
[[Category: Virus/viral protein receptor]]
[[Category: Virus/viral protein receptor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:52:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:24:40 2008''

Revision as of 21:24, 30 June 2008

Image:1eaj.png

Template:STRUCTURE 1eaj

DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN AT 1.35 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 11080637

About this Structure

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

Reference

Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution., van Raaij MJ, Chouin E, van der Zandt H, Bergelson JM, Cusack S, Structure. 2000 Nov 15;8(11):1147-55. PMID:11080637

Page seeded by OCA on Tue Jul 1 00:24:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eaj"
Personal tools