1F5W

DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN

Summary for 1F5W

• Entry DOI: 10.2210/pdb1f5w/pdb
• Related: 1KAC
• Descriptor: COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR, SULFATE ION (3 entities in total)
• Functional Keywords: immunoglobulin v domain fold, symmetric dimer, viral protein receptor
• 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: 2
• Total formula weight: 28386.13

Authors

van Raaij, M.J.,Chouin, E.,van der Zandt, H.,Bergelson, J.M.,Cusack, S. (deposition date: 2000-06-18, release date: 2000-11-08, Last modification date: 2024-11-13)

Primary citation

van Raaij, M.J.,Chouin, E.,van der Zandt, H.,Bergelson, J.M.,Cusack, S.
Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution.
Structure Fold.Des., 8:1147-1155, 2000

PubMed Abstract: The coxsackievirus and adenovirus receptor (CAR) comprises two extracellular immunoglobulin domains, a transmembrane helix and a C-terminal intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is necessary and sufficient for adenovirus binding, whereas the site of coxsackievirus attachment has not yet been localized. The normal cellular role of CAR is currently unknown, although CAR was recently proposed to function as a homophilic cell adhesion molecule.

PubMed: 11080637
DOI: 10.1016/S0969-2126(00)00528-1

Experimental method

X-RAY DIFFRACTION (1.7 Å)