The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures

Structure

Volumn 10, Issue 5, 2002, Pages 673-686

  Barrientos, Laura G ^a   Louis, John M ^a   Botos, Istvan ^b   Mori, Toshiyuki ^b   Han, Zhaozhong ^b   O'Keefe, Barry R ^b   Boyd, Michael R ^b   Wlodawer, Alexander ^b   Gronenborn, Angela M ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

3D domain swapping; Cyanovirin N; NMR; Protein folding; X ray

Indexed keywords

CYANOVIRIN N; DIMER; MONOMER; MUTANT PROTEIN; PROLINE; SERINE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; BACTERIAL PROTEIN; CARRIER PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; GENE MUTATION; KINETICS; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; ROOM TEMPERATURE; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; GENETICS; PROTEIN TERTIARY STRUCTURE;

ANTI-HIV AGENTS; CARRIER PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUPPORT, NON-U.S. GOV'T; BACTERIAL PROTEINS;

RNA VIRUSES;

EID: 0036113691     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00758-X     Document Type: Article

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