D Xia1, L J Henry, R D Gerard, J Deisenhofer. 1. Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas 75235-9050.
Abstract
BACKGROUND: Adenoviral infection begins with the binding of virion to the surface of host cells. Specific attachment is achieved through interactions between host-cell receptors and the adenovirus fiber protein and is mediated by the globular carboxy-terminal domain of the adenovirus fiber protein, termed the carboxy-terminal knob domain. RESULTS: The crystal structure of the carboxy-terminal knob domain of the adenovirus type 5 (Ad5) fiber protein has been determined at 1.7 A resolution. Each knob monomer forms an eight-stranded antiparallel beta-sandwich structure. In the crystal lattice, the knob monomers form closely interacting trimers which possess a deep surface depression centered around the three-fold molecular symmetry axis and three symmetry-related valleys. CONCLUSIONS: The amino acid residues lining the wall of the central surface depression and the three symmetry-related floors of the valleys are strictly conserved in the knob domains of Ad5 and adenovirus type 2 (Ad2) fiber proteins, which share the same cellular receptor. The beta-sandwich structure of the knob monomer demonstrates a unique folding topology which is different from that of other known antiparallel beta-sandwich structures. The large buried surface area and numerous polar interactions in the trimer indicate that this form of the knob protein is predominant in solution, suggesting a possible assembly pathway for the native fiber protein.
BACKGROUND:Adenoviral infection begins with the binding of virion to the surface of host cells. Specific attachment is achieved through interactions between host-cell receptors and the adenovirus fiber protein and is mediated by the globular carboxy-terminal domain of the adenovirus fiber protein, termed the carboxy-terminal knob domain. RESULTS: The crystal structure of the carboxy-terminal knob domain of the adenovirus type 5 (Ad5) fiber protein has been determined at 1.7 A resolution. Each knob monomer forms an eight-stranded antiparallel beta-sandwich structure. In the crystal lattice, the knob monomers form closely interacting trimers which possess a deep surface depression centered around the three-fold molecular symmetry axis and three symmetry-related valleys. CONCLUSIONS: The amino acid residues lining the wall of the central surface depression and the three symmetry-related floors of the valleys are strictly conserved in the knob domains of Ad5 and adenovirus type 2 (Ad2) fiber proteins, which share the same cellular receptor. The beta-sandwich structure of the knob monomer demonstrates a unique folding topology which is different from that of other known antiparallel beta-sandwich structures. The large buried surface area and numerous polar interactions in the trimer indicate that this form of the knob protein is predominant in solution, suggesting a possible assembly pathway for the native fiber protein.
Authors: Nikolay Korokhov; Galina Mikheeva; Alexander Krendelshchikov; Natalya Belousova; Vera Simonenko; Valentina Krendelshchikova; Alexander Pereboev; Alexander Kotov; Olga Kotova; Pierre L Triozzi; Wayne A Aldrich; Joanne T Douglas; Kin-Ming Lo; Papia T Banerjee; Stephen D Gillies; David T Curiel; Victor Krasnykh Journal: J Virol Date: 2003-12 Impact factor: 5.103
Authors: Abhimanyu K Singh; Thanh H Nguyen; Márton Z Vidovszky; Balázs Harrach; Mária Benkő; Alan Kirwan; Lokesh Joshi; Michelle Kilcoyne; M Álvaro Berbis; F Javier Cañada; Jesús Jiménez-Barbero; Margarita Menéndez; Sarah S Wilson; Beth A Bromme; Jason G Smith; Mark J van Raaij Journal: J Gen Virol Date: 2018-10-02 Impact factor: 3.891