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.

3jz7

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 14:20, 25 December 2014

Crystal structure of the extracellular domains of coxsackie & adenovirus receptor from mouse (mCAR)

Structural highlights

3jz7 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1kac, 1f5w, 1eaj, 1jew, 2wbw, 2npl
Gene:	Car, Cxadr (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CXAR_MOUSE] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN (By similarity).^[1] ^[2] ^[3] In vitro, acts as a receptor for group B coxsackieviruses and subgroup C of adenoviruses (AD2 and AD5).^[4] ^[5] ^[6]

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 coxsackievirus-adenovirus receptor (CAR) is a member of the Ig superfamily strongly expressed in the developing nervous system. Our histological investigations during development reveal an initial uniform distribution of CAR on all neural cells with a concentration on membranes that face the margins of the nervous system (e.g., the basal laminae and the ventricular side). At more advanced stages, CAR becomes downregulated and restricted to specific regions including areas rich in axonal and dendritic surfaces. To study the function of CAR on neural cells, we used the fiber knob of the adenovirus, extracellular CAR domains, blocking antibodies to CAR, as well as CAR-deficient neural cells. Blocking antibodies were found to inhibit neurite extension in retina organ and retinal explant cultures, whereas the application of the recombinant fiber knob of the adenovirus subtype Ad2 or extracellular CAR domains promoted neurite extension and adhesion to extracellular matrices. We observed a promiscuous interaction of CAR with extracellular matrix glycoproteins, which was deduced from analytical ultracentrifugation experiments, affinity chromatography, and adhesion assays. The membrane proximal Ig domain of CAR, termed D2, was found to bind to a fibronectin fragment, including the heparin-binding domain 2, which promotes neurite extension of wild type, but not of CAR-deficient neural cells. In contrast to heterophilic interactions, homophilic association of CAR involves both Ig domains, as was revealed by ultracentrifugation, chemical cross-linking, and adhesion studies. The results of these functional and binding studies are correlated to a U-shaped homodimer of the complete extracellular domains of CAR detected by x-ray crystallography.

The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells.,Patzke C, Max KE, Behlke J, Schreiber J, Schmidt H, Dorner AA, Kroger S, Henning M, Otto A, Heinemann U, Rathjen FG J Neurosci. 2010 Feb 24;30(8):2897-910. PMID:20181587^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 1997 Feb 28;275(5304):1320-3. PMID:9036860
↑ Bergelson JM, Krithivas A, Celi L, Droguett G, Horwitz MS, Wickham T, Crowell RL, Finberg RW. The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses. J Virol. 1998 Jan;72(1):415-9. PMID:9420240
↑ Honda T, Saitoh H, Masuko M, Katagiri-Abe T, Tominaga K, Kozakai I, Kobayashi K, Kumanishi T, Watanabe YG, Odani S, Kuwano R. The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain. Brain Res Mol Brain Res. 2000 Apr 14;77(1):19-28. PMID:10814828
↑ Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 1997 Feb 28;275(5304):1320-3. PMID:9036860
↑ Bergelson JM, Krithivas A, Celi L, Droguett G, Horwitz MS, Wickham T, Crowell RL, Finberg RW. The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses. J Virol. 1998 Jan;72(1):415-9. PMID:9420240
↑ Honda T, Saitoh H, Masuko M, Katagiri-Abe T, Tominaga K, Kozakai I, Kobayashi K, Kumanishi T, Watanabe YG, Odani S, Kuwano R. The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain. Brain Res Mol Brain Res. 2000 Apr 14;77(1):19-28. PMID:10814828
↑ Patzke C, Max KE, Behlke J, Schreiber J, Schmidt H, Dorner AA, Kroger S, Henning M, Otto A, Heinemann U, Rathjen FG. The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells. J Neurosci. 2010 Feb 24;30(8):2897-910. PMID:20181587 doi:30/8/2897

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3jz7"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jz7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jz7 RCSB], [http://www.ebi.ac.uk/pdbsum/3jz7 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CXAR_MOUSE CXAR_MOUSE]] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN (By similarity).<ref>PMID:9036860</ref> <ref>PMID:9420240</ref> <ref>PMID:10814828</ref>   In vitro, acts as a receptor for group B coxsackieviruses and subgroup C of adenoviruses (AD2 and AD5).<ref>PMID:9036860</ref> <ref>PMID:9420240</ref> <ref>PMID:10814828</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3jz7

From Proteopedia

Revision as of 14:20, 25 December 2014

Crystal structure of the extracellular domains of coxsackie & adenovirus receptor from mouse (mCAR)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox