1rsf
From Proteopedia
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'''NMR Structure of Monomeric CAR d1 domain''' | '''NMR Structure of Monomeric CAR d1 domain''' | ||
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[[Category: Jiang, S.]] | [[Category: Jiang, S.]] | ||
[[Category: Laue, T M.]] | [[Category: Laue, T M.]] | ||
- | [[Category: | + | [[Category: Adenovirus]] |
- | [[Category: | + | [[Category: Car]] |
- | [[Category: | + | [[Category: Coxsackievirus]] |
- | [[Category: | + | [[Category: Nmr]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:51:21 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 04:51, 3 May 2008
NMR Structure of Monomeric CAR d1 domain
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.
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 Sat May 3 07:51:21 2008
Categories: Homo sapiens | Single protein | Caffrey, M. | Jacobs, A. | Jiang, S. | Laue, T M. | Adenovirus | Car | Coxsackievirus | Nmr