Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects.
Biochimie
; 74(9-10): 825-36, 1992.
Article
en En
| MEDLINE
| ID: mdl-1467342
2-D and 3-D NMR techniques were used to investigate the conformations in solution of several peptides and proteins for which crystalline structures are not available yet. Insect defensin A is a small (40 aa) antibiotic protein exhibiting a characteristic 'loop-helix-beta-sheet' structure. A striking analogy was found with charybdotoxin, a scorpion toxin in which a CSH (cysteine stabilized alpha-helix) motif is also present. Wheat phospholipid transfer protein (PLTP) (90 aa) has a 3-D structure resulting from the packing of four helices and of a C-terminal less well-defined fragment. Preliminary results show that PLTP forms a complex with lyso-PC and that such an interaction results in a conformational change affecting principally the C-terminal half of the protein. A last example is given with surfactin, a lipopeptide biosurfactant from bacterial origin. Its protonated form shows a very compact structure in which the two acidic residues located on the top of a 'horse saddle' topology face each other, whereas the ionized form could adopt a more extended conformation. A common property of these compounds is their capacity to interact with lipids. The present structural data open the way for a further establishment of structure-activity relationships.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Péptidos Cíclicos
/
Espectroscopía de Resonancia Magnética
/
Proteínas
/
Defensinas
/
Proteínas de Transferencia de Fosfolípidos
/
Hormonas de Insectos
Idioma:
En
Revista:
Biochimie
Año:
1992
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Francia