2RDK

Five site mutated Cyanovirin-N with Mannose dimer bound

Summary for 2RDK

• Entry DOI: 10.2210/pdb2rdk/pdb
• Related: 1IIY 1LOM 1M5M 2PYS 2Z21 3EZM
• Related PRD ID: PRD_900111
• Descriptor: Cyanovirin-N, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose (3 entities in total)
• Functional Keywords: cyanovirin-n, sugar binding protein, anti hiv, antiviral protein, protein synthesis inhibitor
• Biological source: Nostoc ellipsosporum
• Total number of polymer chains: 2
• Total formula weight: 24582.78

Authors

Fromme, R.,Katiliene, Z.,Fromme, P.,Ghirlanda, G. (deposition date: 2007-09-24, release date: 2008-05-06, Last modification date: 2024-11-06)

Primary citation

Fromme, R.,Katiliene, Z.,Fromme, P.,Ghirlanda, G.
Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution.
Protein Sci., 17:939-944, 2008

PubMed Abstract: Cyanovirin (CV-N) is a small lectin with potent HIV neutralization activity, which could be exploited for a mucosal defense against HIV infection. The wild-type (wt) protein binds with high affinity to mannose-rich oligosaccharides on the surface of gp120 through two quasi-symmetric sites, located in domains A and B. We recently reported on a mutant of CV-N that contained a single functional mannose-binding site, domain B, showing that multivalent binding to oligomannosides is necessary for antiviral activity. The structure of the complex with dimannose determined at 1.8 A resolution revealed a different conformation of the binding site than previously observed in the NMR structure of wt CV-N. Here, we present the 1.35 A resolution structure of the complex, which traps three different binding conformations of the site and provides experimental support for a locking and gating mechanism in the nanoscale time regime observed by molecular dynamics simulations.

PubMed: 18436959
DOI: 10.1110/ps.083472808

Experimental method

X-RAY DIFFRACTION (1.35 Å)