1H7Z

Adenovirus Ad3 fibre head

Summary for 1H7Z

• Entry DOI: 10.2210/pdb1h7z/pdb
• Related: 1KNB
• Descriptor: ADENOVIRUS FIBRE PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: cell receptor recognition, adenovirus, ad3, fibre, receptor
• Biological source: HUMAN ADENOVIRUS TYPE 3
• Total number of polymer chains: 3
• Total formula weight: 65524.85

Authors

Durmort, C.,Stehlin, C.,Schoehn, G.,Mitraki, A.,Drouet, E.,Cusack, S.,Burmeister, W.P. (deposition date: 2001-01-21, release date: 2001-07-19, Last modification date: 2023-12-13)

Primary citation

Durmort, C.,Stehlin, C.,Schoehn, G.,Mitraki, A.,Drouet, E.,Cusack, S.,Burmeister, W.P.
Structure of the Fiber Head of Ad3, a Non-Car-Binding Serotype of Adenovirus
Virology, 285:302-, 2001

PubMed Abstract: Adenoviruses of serotype Ad3 (subgenus B) use a still-unknown host cell receptor for viral attachment, whereas viruses from all other known subgenera use the coxsackie and adenovirus receptor (CAR). The receptor binding domain (head) of the Ad3 fiber protein has been expressed in Escherichia coli inclusion bodies. After denaturation and renaturation using a rapid dilution method, crystals of trimeric head were obtained. The 1.6 A resolution X-ray structure shows a strict conservation of the beta-sheet scaffold of the protein very similar to the head structures of the CAR-binding serotypes Ad2, Ad5, and Ad12. The conformation of the loops is different, with the exception of the AB loop, which forms the center of the interface in the Ad12-CAR complex structure. The structure explains why a mutation in Ad5 of one residue in the AB loop to glutamic acid, as in Ad3, abrogates binding to CAR. It is possible that the Ad3 receptor binding site is nevertheless situated similar to the CAR binding site, although it cannot be excluded that other regions of the relatively hydrophobic head surface may be used.

PubMed: 11437664
DOI: 10.1006/VIRO.2001.0967

Experimental method

X-RAY DIFFRACTION (1.6 Å)