Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1

Shaokai Jiang; Amy Jacobs; Thomas M. Laue; Michael Caffrey

doi:10.1021/bi035490x

Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1

Shaokai Jiang
, Amy Jacobs
, Thomas M. Laue
, Michael Caffrey

Microbiology and Immunology

University of Illinois at Chicago
University of New Hampshire

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	1847-1853
Number of pages	7
Journal	Biochemistry
Volume	43
Issue number	7
DOIs	https://doi.org/10.1021/bi035490x
State	Published - Feb 24 2004

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title = "Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1",

abstract = "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.",

author = "Shaokai Jiang and Amy Jacobs and Laue, \{Thomas M.\} and Michael Caffrey",

year = "2004",

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AU - Laue, Thomas M.

AU - Caffrey, Michael

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Y1 - 2004/2/24

N2 - 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.

AB - 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.

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DO - 10.1021/bi035490x

M3 - Article

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AN - SCOPUS:1242307802

SN - 0006-2960

VL - 43

SP - 1847

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JO - Biochemistry

JF - Biochemistry

IS - 7

ER -

Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1

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