2MWT

NMR structure of crotalicidin in DPC micelles

2MWT の概要

• エントリーDOI: 10.2210/pdb2mwt/pdb
• NMR情報: BMRB: 25363
• 分子名称: Cathelicidin-like peptide (1 entity in total)
• 機能のキーワード: antimicrobial peptide, antitumor peptide, antimicrobial protein, antitumor protein, antimicrobial
• 由来する生物種: Crotalus durissus terrificus (South American rattlesnake,cascabel)
• 細胞内の位置: Secreted : U5KJM4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4167.42

構造登録者

Jimenez, M.,Zamora-Carreras, H. (登録日: 2014-11-24, 公開日: 2015-11-04, 最終更新日: 2024-05-15)

主引用文献

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

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: 26465972
DOI: 10.1021/acs.jmedchem.5b01142

実験手法

SOLUTION NMR