2MWT
NMR structure of crotalicidin in DPC micelles
Summary for 2MWT
| Entry DOI | 10.2210/pdb2mwt/pdb |
| NMR Information | BMRB: 25363 |
| Descriptor | Cathelicidin-like peptide (1 entity in total) |
| Functional Keywords | antimicrobial peptide, antitumor peptide, antimicrobial protein, antitumor protein, antimicrobial |
| Biological source | Crotalus durissus terrificus (South American rattlesnake,cascabel) |
| Cellular location | Secreted : U5KJM4 |
| Total number of polymer chains | 1 |
| Total formula weight | 4167.42 |
| Authors | Jimenez, M.,Zamora-Carreras, H. (deposition date: 2014-11-24, release date: 2015-11-04, Last modification date: 2024-05-15) |
| Primary citation | Falcao, C.B.,Perez-Peinado, C.,de la Torre, B.G.,Mayol, X.,Zamora-Carreras, H.,Jimenez, M.A.,Radis-Baptista, G.,Andreu, D. Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity. J.Med.Chem., 58:8553-8563, 2015 Cited by PubMed Abstract: In silico dissection of crotalicidin (Ctn), a cathelicidin from a South American pit viper, yielded fragments Ctn[1-14] and Ctn[15-34], which were tested to ascertain to what extent they reproduced the structure and activity of the parent peptide. NMR data showing Ctn to be α-helical at the N-terminus and unstructured at the C-terminus were matched by similar data from the fragments. The peptides were tested against Gram-positive and -negative bacteria and for toxicity against both tumor and healthy cells. Despite its amphipathic α-helical structure, Ctn[1-14] was totally inert toward bacteria or eukaryotic cells. In contrast, unstructured Ctn[15-34] replicated the activity of parent Ctn against Gram-negative bacteria and tumor cells while being significantly less toxic toward eukaryotic cells. This selectivity for bacteria and tumor cells, plus a stability to serum well above that of Ctn, portrays Ctn[15-34] as an appealing candidate for further development as an anti-infective or antitumor lead. PubMed: 26465972DOI: 10.1021/acs.jmedchem.5b01142 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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