Solution structure of cyanovirin-N, a potent HIV-inactivating protein
| Autor: | Carole A. Bewley, D G Covell, Angela M. Gronenborn, G M Clore, Ad Bax, Michael R. Boyd, Kirk R. Gustafson |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Stereochemistry Anti-HIV Agents Molecular Sequence Data Human immunodeficiency virus (HIV) Sequence alignment medicine.disease_cause Crystallography X-Ray Biochemistry Protein Structure Secondary Protein structure Bacterial Proteins Structural Biology Genetics medicine Amino Acid Sequence Binding site Peptide sequence Nuclear Magnetic Resonance Biomolecular Binding Sites biology Nuclear magnetic resonance spectroscopy Solution structure Protein Structure Tertiary Crystallography Cyanovirin-N biology.protein Carrier Proteins Sequence Alignment |
| Zdroj: | Nature structural biology. 5(7) |
| ISSN: | 1072-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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