1knb

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PDB ID 1knb

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, resolution 1.7Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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 5. 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

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