1KAC

KNOB DOMAIN FROM ADENOVIRUS SEROTYPE 12 IN COMPLEX WITH DOMAIN 1 OF ITS CELLULAR RECEPTOR CAR

Summary for 1KAC

• Entry DOI: 10.2210/pdb1kac/pdb
• Related: 1NOB
• Descriptor: PROTEIN (FIBER KNOB PROTEIN), PROTEIN (COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR) (3 entities in total)
• Functional Keywords: adhesion protein receptor complex, viral protein-receptor complex, viral protein/receptor
• Biological source: Human adenovirus 12; More
• 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: 33584.98

Authors

Bewley, M.C.,Springer, K.,Zhang, Y.B.,Freimuth, P.,Flanagan, J.M. (deposition date: 1999-05-05, release date: 1999-11-24, Last modification date: 2023-12-27)

Primary citation

Bewley, M.C.,Springer, K.,Zhang, Y.B.,Freimuth, P.,Flanagan, J.M.
Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.
Science, 286:1579-1583, 1999

PubMed Abstract: Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors.

PubMed: 10567268
DOI: 10.1126/science.286.5444.1579

Experimental method

X-RAY DIFFRACTION (2.6 Å)