2ezn
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SOLUTION NMR STRUCTURE OF CYANOVIRIN-N ENSEMBLE OF 40 SIMULATED ANNEALING STRUCTURES
OverviewOverview
The solution structure of cyanovirin-N, a potent 11,000 Mr, HIV-inactivating protein that binds with high affinity and specificity to, the HIV surface envelope protein gp120, has been solved by nuclear, magnetic resonance spectroscopy, including extensive use of dipolar, couplings which provide a priori long range structural information., Cyanovirin-N is an elongated, largely beta-sheet protein that displays, internal two-fold pseudosymmetry. The two sequence repeats (residues 1-50, and 51-101) share 32% sequence identity and superimpose with a backbone, atomic root-mean-square difference of 1.3 A. The two repeats, however, do, not form separate domains since the overall fold is dependent on numerous, contacts between them. Rather, two symmetrically related domains are, formed by strand exchange between the two repeats. Analysis of surface, hydrophobic clusters suggests the location of potential binding sites for, protein-protein interactions.
About this StructureAbout this Structure
2EZN is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of cyanovirin-N, a potent HIV-inactivating protein., Bewley CA, Gustafson KR, Boyd MR, Covell DG, Bax A, Clore GM, Gronenborn AM, Nat Struct Biol. 1998 Jul;5(7):571-8. PMID:9665171
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