2jq2
From Proteopedia
NMR structure of the anticoccidial peptide PW2 in DPC micelles
Overview
PW2 is an anticoccidial peptide active against Eimeria acervulina and Eimeria tenella. We determined the structure of PW2 in dodecylphosphocholine micelles. The structure showed two distinct regions: an amphipathic N-terminal 3(10) helix and an aromatic region containing WWR interface-binding motif. The aromatic region acted as a scaffold of the protein in the interface and shared the same structure in both DPC and SDS micelles. N-terminal helix interacted with DPC but not with SDS interface. Chemical shift change was slow when SDS was added to PW2 in DPC and fast when DPC was added to PW2 in SDS, indicating that interaction with DPC micelles was kinetically more stable than with SDS micelles. Also, DPC interface was able to accommodate PW2, but it maintained the conformational arrangement in the aromatic region observed for SDS micelles. This behavior, which is different from that observed for other antimicrobial peptides with WWR motif, may be associated with the absence of PW2 antibacterial activity and its selectivity for Eimeria parasites.
About this Structure
Full crystallographic information is available from OCA.
Reference
Effect of micelle interface on the binding of anticoccidial PW2 peptide., Tinoco LW, Gomes-Neto F, Valente AP, Almeida FC, J Biomol NMR. 2007 Dec;39(4):315-22. Epub 2007 Oct 10. PMID:17926009 Page seeded by OCA on Sun May 4 09:10:17 2008
