2LYF

High resolution NMR solution structure of the theta-defensin RTD-1

Summary for 2LYF

• Entry DOI: 10.2210/pdb2lyf/pdb
• Related: 1HVZ 2ATG 2LYE
• NMR Information: BMRB: 18723
• Descriptor: RTD-1 (1 entity in total)
• Functional Keywords: theta-defensin, cyclic peptides, cyclic cystine ladder, antimicrobial protein
• Total number of polymer chains: 1
• Total formula weight: 2110.67

Authors

Conibear, A.C.,Rosengren, K.,Harvey, P.J.,Craik, D.J. (deposition date: 2012-09-18, release date: 2012-11-28, Last modification date: 2024-11-13)

Primary citation

Conibear, A.C.,Rosengren, K.J.,Harvey, P.J.,Craik, D.J.
Structural characterization of the cyclic cystine ladder motif of theta-defensins.
Biochemistry, 51:9718-9726, 2012

PubMed Abstract: The θ-defensins are, to date, the only known ribosomally synthesized cyclic peptides in mammals, and they have promising antimicrobial bioactivities. The characteristic structural motif of the θ-defensins is the cyclic cystine ladder, comprising a cyclic peptide backbone and three parallel disulfide bonds. In contrast to the cyclic cystine knot, which characterizes the plant cyclotides, the cyclic cystine ladder has not been as well described as a structural motif. Here we report the solution structures and nuclear magnetic resonance relaxation properties in aqueous solution of three representative θ-defensins from different species. Our data suggest that the θ-defensins are more rigid and structurally defined than previously thought. In addition, all three θ-defensins were found to self-associate in aqueous solution in a concentration-dependent and reversible manner, a property that might have a role in their mechanism of action. The structural definition of the θ-defensins and the cyclic cystine ladder will help to guide exploitation of these molecules as structural frameworks for the design of peptide drugs.

PubMed: 23148585
DOI: 10.1021/bi301363a

Experimental method

SOLUTION NMR