2JMV

Solution structure of scytovirin refined against residual dipolar couplings

Summary for 2JMV

• Entry DOI: 10.2210/pdb2jmv/pdb
• Descriptor: Scytovirin (1 entity in total)
• Functional Keywords: protein, sugar binding protein, antiviral protein
• Biological source: Scytonema varium
• Total number of polymer chains: 1
• Total formula weight: 9733.50

Authors

McFeeters, R.L.,Byrd, R.A. (deposition date: 2006-12-07, release date: 2007-06-12, Last modification date: 2024-11-20)

Primary citation

McFeeters, R.L.,Xiong, C.,O'Keefe, B.R.,Bokesch, H.R.,McMahon, J.B.,Ratner, D.M.,Castelli, R.,Seeberger, P.H.,Byrd, R.A.
The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors
J.Mol.Biol., 369:451-461, 2007

PubMed 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 carbohydrate-binding proteins but differing in carbohydrate specificity. Scytovirin, originally isolated from the cyanobacterium Scytonema varium, holds potential as an HIV entry inhibitor for both therapeutic and prophylactic anti-HIV applications. The high-resolution structural studies reported are an important initial step in unlocking the therapeutic potential of scytovirin.

PubMed: 17434526
DOI: 10.1016/j.jmb.2007.03.030

Experimental method

SOLUTION NMR