1IIY
Solution NMR Structure of Complex of 1:2 Cyanovirin-N:Man-Alpha1,2-Man-Alpha Restrained Regularized Mean Coordinates
Summary for 1IIY
Entry DOI | 10.2210/pdb1iiy/pdb |
Related PRD ID | PRD_900111 |
Descriptor | CYANOVIRIN-N, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose (2 entities in total) |
Functional Keywords | hiv-inactivating protein, man-alpha1, 2-man-alpha, antiviral protein |
Biological source | Nostoc ellipsosporum |
Total number of polymer chains | 1 |
Total formula weight | 11706.68 |
Authors | Bewley, C.A. (deposition date: 2001-04-24, release date: 2001-10-24, Last modification date: 2020-07-29) |
Primary citation | Bewley, C.A. Solution Structure of a Cyanovirin-N:Man alpha 1-2Man alpha Complex. Structural Basis for High Affinity Carbohydrate-Mediated Binding to gp120 Structure, 9:931-940, 2001 Cited by PubMed Abstract: Cyanovirin-N (CVN) is a novel, 11 kDa cyanobacterial protein that potently inhibits viral entry by diverse strains of HIV through high-affinity carbohydrate-mediated interactions with the viral envelope glycoprotein gp120. CVN contains two symmetry-related carbohydrate binding sites of differing affinities that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinities, the carbohydrates that also mediate CVN:gp120 binding. High-resolution structural studies of CVN in complex with a representative oligosaccharide are desirable for understanding the structural basis for this unprecedented specificity. PubMed: 11591348DOI: 10.1016/S0969-2126(01)00653-0 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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