Solution Structure of a Cyanovirin-N:Manα1-2Manα Complex
- 1 October 2001
- Vol. 9 (10), 931-940
- https://doi.org/10.1016/s0969-2126(01)00653-0
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- The Potent Anti-HIV Protein Cyanovirin-N Contains Two Novel Carbohydrate Binding Sites That Selectively Bind to Man8 D1D3 and Man9 with Nanomolar Affinity: Implications for Binding to the HIV Envelope Protein gp120Journal of the American Chemical Society, 2001
- Analysis of the Interaction between the HIV-Inactivating Protein Cyanovirin-N and Soluble Forms of the Envelope Glycoproteins gp120 and gp41Molecular Pharmacology, 2000
- Determination of the Relative Orientation of the Two Halves of the Domain-Swapped Dimer of Cyanovirin-N in Solution Using Dipolar Couplings and Rigid Body MinimizationJournal of the American Chemical Society, 2000
- Multiple Antiviral Activities of Cyanovirin-N: Blocking of Human Immunodeficiency Virus Type 1 gp120 Interaction with CD4 and Coreceptor and Inhibition of Diverse Enveloped VirusesJournal of Virology, 2000
- Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swappingJournal of Molecular Biology, 1999
- Simplified procedure for fractionation and structural characterisation of complex mixtures of N-linked glycans, released from HIV-1 gp120 and other highly glycosylated viral proteins.Journal of Virological Methods, 1998
- Solution structure of cyanovirin-N, a potent HIV-inactivating proteinNature Structural & Molecular Biology, 1998
- HIV Entry and Its InhibitionCell, 1998
- Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline MediumScience, 1997
- Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide developmentAntimicrobial Agents and Chemotherapy, 1997