A proposed 3D structure for crotamine based on homology building, molecular simulations and circular dichroism.
Crotamine, isolated from the venom of the South American rattlesnake Crotalus durissus terrificus is a strongly basic 42-amino acid polypeptide belonging to the small basic myotoxin family. As no tridimensional structure is available for this myotoxin subfamily, despite its important pharmacological interest, we propose in this paper a theoretical 3D model for crotamine. Starting from a homology modelling procedure, followed by intensive molecular dynamics (MD) simulations in water and complementary CD experiments, the designed 3D model is the first example of a tridimensional structure in this family of small basic myotoxins. Crotamine, therefore, belongs to a newly identified structural family presenting a common fold also found in beta-defensin and antopleurine-B. The proposed 3D model will be used for future calculations about crotamine aggregation and interaction with membranes.
Siqueira
A M
AM
Department of Biochemistry and Immunology, Federal University of Minas Gerais, Belo Horizonte, Brazil.
Martins
N F
NF
De Lima
M E
ME
Diniz
C R
CR
Cartier
A
A
Brown
D
D
Maigret
B
B
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D003196:Computer Graphics; D003435:Crotalid Venoms / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
D003435:Crotalid Venoms; C010563:crotamine