The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors.

ABSTRACT: The solution structure of the potent 95 residue anti-HIV protein scytovirin has been determined and two carbohydrate-binding sites have been identified. This unique protein, containing five structurally important disulfide bonds, demonstrates a novel fold with no elements of extended regular secondary structure. Scytovirin contains two 39 residue sequence repeats, differing in only three amino acid residues, and each repeat has primary sequence similarity to chitin binding proteins. Both sequence repeats form similarly structured domains, with the exception of one region. The result is two carbohydrate-binding sites with substantially different affinities. The unusual fold clusters aromatic residues in both sites, suggesting a binding mechanism similar to other known hevein-like carbohydra

SUBMITTER: McFeeters RL 

PROVIDER: S-EPMC2696897 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature