2M2X
Solution structure of the antimicrobial peptide [Aba3,5,7,12,14,16]BTD-2
Summary for 2M2X
| Entry DOI | 10.2210/pdb2m2x/pdb |
| Related | 2M1P 2M2G 2M2H 2M2S 2M2Y 2lye |
| NMR Information | BMRB: 18937 |
| Related PRD ID | PRD_001009 |
| Descriptor | [Aba3,5,7,12,14,16]BTD-2 (1 entity in total) |
| Functional Keywords | theta-defensin, cyclic peptides, cyclic cystine ladder, disulfide bond, antimicrobial peptide, antimicrobial protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 1982.43 |
| Authors | Conibear, A.C.,Rosengren, K.,Daly, N.L.,Troiera Henriques, S.,Craik, D.J. (deposition date: 2013-01-03, release date: 2013-02-27, Last modification date: 2023-11-15) |
| Primary citation | Conibear, A.C.,Rosengren, K.J.,Daly, N.L.,Henriques, S.T.,Craik, D.J. The cyclic cystine ladder in theta-defensins is important for structure and stability, but not antibacterial activity. J.Biol.Chem., 288:10830-10840, 2013 Cited by PubMed Abstract: θ-Defensins are ribosomally synthesized cyclic peptides found in the leukocytes of some primate species and have promising applications as antimicrobial agents and scaffolds for peptide drugs. The cyclic cystine ladder motif, comprising a cyclic peptide backbone and three parallel disulfide bonds, is characteristic of θ-defensins. In this study, we explore the role of the cyclic peptide backbone and cystine ladder in the structure, stability, and activity of θ-defensins. θ-Defensin analogues with different numbers and combinations of disulfide bonds were synthesized and characterized in terms of their NMR solution structures, serum and thermal stabilities, and their antibacterial and membrane-binding activities. Whereas the structures and stabilities of the peptides were primarily dependent on the number and position of the disulfide bonds, their antibacterial and membrane-binding properties were dependent on the cyclic backbone. The results provide insights into the mechanism of action of θ-defensins and illustrate the potential of θ-defensin analogues as scaffolds for peptide drug design. PubMed: 23430740DOI: 10.1074/jbc.M113.451047 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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