4GV5

X-ray structure of crotamine, a cell-penetrating peptide from the Brazilian snake Crotalus durissus terrificus

Summary for 4GV5

• Entry DOI: 10.2210/pdb4gv5/pdb
• Descriptor: Crotamine Ile-19, THIOCYANATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: alpha helix & beta sheet, ion channel inhibitor, antibacterial peptide, extracellular region, toxin
• Biological source: Crotalus durissus terrificus (South American rattlesnake)
• Total number of polymer chains: 3
• Total formula weight: 15597.53

Authors

Coronado, M.A.,Gabdulkhakov, A.,Georgieva, D.,Sankaran, B.,Murakami, M.T.,Arni, R.K.,Betzel, C. (deposition date: 2012-08-30, release date: 2013-09-04, Last modification date: 2024-11-20)

Primary citation

Coronado, M.A.,Gabdulkhakov, A.,Georgieva, D.,Sankaran, B.,Murakami, M.T.,Arni, R.K.,Betzel, C.
Structure of the polypeptide crotamine from the Brazilian rattlesnake Crotalus durissus terrificus.
Acta Crystallogr.,Sect.D, 69:1958-1964, 2013

PubMed Abstract: The crystal structure of the myotoxic, cell-penetrating, basic polypeptide crotamine isolated from the venom of Crotalus durissus terrificus has been determined by single-wavelength anomalous dispersion techniques and refined at 1.7 Å resolution. The structure reveals distinct cationic and hydrophobic surface regions that are located on opposite sides of the molecule. This surface-charge distribution indicates its possible mode of interaction with negatively charged phospholipids and other molecular targets to account for its diverse pharmacological activities. Although the sequence identity between crotamine and human β-defensins is low, the three-dimensional structures of these functionally related peptides are similar. Since crotamine is a leading member of a large family of myotoxic peptides, its structure will provide a basis for the design of novel cell-penetrating molecules.

PubMed: 24100315
DOI: 10.1107/S0907444913018003

Experimental method

X-RAY DIFFRACTION (1.7 Å)