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 Å 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 Å 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.
Original language | English (US) |
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Pages (from-to) | 939-944 |
Number of pages | 6 |
Journal | Protein Science |
Volume | 17 |
Issue number | 5 |
DOIs | |
State | Published - May 2008 |
Keywords
- Antiviral protein
- Cyanovirin
- Lectins
- Sugar binding
- X-ray structure analysis
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
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Dive into the research topics of 'Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 Å resolution'. Together they form a unique fingerprint.Datasets
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Five site mutated Cyanovirin-N with Mannose dimer bound
Fromme, R. (Contributor), Katiliene, Z. (Contributor), Fromme, P. (Contributor), Ghirlanda, G. (Contributor), Giomarelli, B. (Contributor), Bogani, F. (Contributor), Mc Mahon, J. (Contributor) & Mori, T. (Contributor), Protein Data Bank (PDB), May 6 2008
DOI: 10.2210/pdb2RDK/pdb, https://www.wwpdb.org/pdb?id=pdb_00002rdk
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