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1knb
From Proteopedia
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CRYSTAL STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF ADENOVIRUS TYPE 5 FIBER PROTEIN AT 1.7 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1KNB is a Single protein structure of sequence from Human adenovirus 11. Full crystallographic information is available from OCA.
Reference
Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution., Xia D, Henry LJ, Gerard RD, Deisenhofer J, Structure. 1994 Dec 15;2(12):1259-70. PMID:7704534
Page seeded by OCA on Tue Nov 20 19:23:58 2007
