1rsf
From Proteopedia
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NMR Structure of Monomeric CAR d1 domain
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Adrenocortical tumor, somatic OMIM:[188830], Carney complex, type 1 OMIM:[188830], Myxoma, intracardiac OMIM:[188830], Pigmented adrenocortical disease, primary, 1 OMIM:[188830], Spastic paraplegia-7 OMIM:[602783], Thyroid carcinoma, papillary OMIM:[188830]
About this Structure
1RSF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:54:01 2008
Categories: Homo sapiens | Single protein | Caffrey, M. | Jacobs, A. | Jiang, S. | Laue, T M. | Adenovirus | Car | Coxsackievirus | Nmr
