1RSF

NMR Structure of Monomeric CAR d1 domain

Summary for 1RSF

• Entry DOI: 10.2210/pdb1rsf/pdb
• Related: 1EAJ
• NMR Information: BMRB: 5516
• Descriptor: Coxsackievirus and adenovirus receptor (1 entity in total)
• Functional Keywords: car, coxsackievirus, adenovirus, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Secreted: P78310
• Total number of polymer chains: 1
• Total formula weight: 13814.65

Authors

Jiang, S.,Jacobs, A.,Laue, T.M.,Caffrey, M. (deposition date: 2003-12-09, release date: 2004-03-02, Last modification date: 2024-10-30)

Primary citation

Jiang, S.,Jacobs, A.,Laue, T.M.,Caffrey, M.
Solution structure of the coxsackievirus and adenovirus receptor domain 1.
Biochemistry, 43:1847-1853, 2004

PubMed 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.

PubMed: 14967025
DOI: 10.1021/bi035490x

Experimental method

SOLUTION NMR