1rsf

NMR Structure of Monomeric CAR d1 domainNMR Structure of Monomeric CAR d1 domain

Structural highlights

1rsf is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 30 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CXAR_HUMAN 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.^[1] ^[2] ^[3] ^[4]

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 and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer-dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure.

Solution structure of the coxsackievirus and adenovirus receptor domain 1.,Jiang S, Jacobs A, Laue TM, Caffrey M Biochemistry. 2004 Feb 24;43(7):1847-53. PMID:14967025^[5]

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

References

↑ Tomko RP, Xu R, Philipson L. HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3352-6. PMID:9096397
↑ Cohen CJ, Shieh JT, Pickles RJ, Okegawa T, Hsieh JT, Bergelson JM. The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15191-6. Epub 2001 Dec 4. PMID:11734628 doi:10.1073/pnas.261452898
↑ Walters RW, Freimuth P, Moninger TO, Ganske I, Zabner J, Welsh MJ. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell. 2002 Sep 20;110(6):789-99. PMID:12297051
↑ Zen K, Liu Y, McCall IC, Wu T, Lee W, Babbin BA, Nusrat A, Parkos CA. Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils. Mol Biol Cell. 2005 Jun;16(6):2694-703. Epub 2005 Mar 30. PMID:15800062 doi:E05-01-0036
↑ Jiang S, Jacobs A, Laue TM, Caffrey M. Solution structure of the coxsackievirus and adenovirus receptor domain 1. Biochemistry. 2004 Feb 24;43(7):1847-53. PMID:14967025 doi:10.1021/bi035490x

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Tomko RP, Xu R, Philipson L. HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3352-6. PMID:9096397

[2] Cohen CJ, Shieh JT, Pickles RJ, Okegawa T, Hsieh JT, Bergelson JM. The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15191-6. Epub 2001 Dec 4. PMID:11734628 doi:10.1073/pnas.261452898

[3] Walters RW, Freimuth P, Moninger TO, Ganske I, Zabner J, Welsh MJ. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell. 2002 Sep 20;110(6):789-99. PMID:12297051

[4] Zen K, Liu Y, McCall IC, Wu T, Lee W, Babbin BA, Nusrat A, Parkos CA. Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils. Mol Biol Cell. 2005 Jun;16(6):2694-703. Epub 2005 Mar 30. PMID:15800062 doi:E05-01-0036

[5] Jiang S, Jacobs A, Laue TM, Caffrey M. Solution structure of the coxsackievirus and adenovirus receptor domain 1. Biochemistry. 2004 Feb 24;43(7):1847-53. PMID:14967025 doi:10.1021/bi035490x

[1]

[2]

[3]

[4]

[5]