5zfo

Publication Abstract from PubMed

Although several plant protease inhibitors have been structurally characterized using X-ray crystallography, very few have been studied using NMR techniques. Here, we report an NMR study of the solution structure and dynamics of an inhibitory repeat domain (IRD) variant 12 from the wound-inducible Pin-II type proteinase inhibitor from Capsicum annuum. IRD variant 12 (IRD12) showed strong anti-metabolic activity against the Lepidopteran insect pest, Helicoverpa armigera. The NMR-derived three-dimensional structure of IRD12 reveals a three-stranded anti-parallel beta-sheet rigidly held together by four disulfide bridges and shows structural homology with known IRDs. It is interesting to note that the IRD12 structure containing approximately 75% unstructured part still shows substantial amount of rigidity of N-H bond vectors with respect to its molecular motion. Communicated by Ramaswamy H. Sarma.

NMR structure and dynamics of inhibitory repeat domain variant 12, a plant protease inhibitor from Capsicum annuum, and its structural relationship to other plant protease inhibitors.,Gartia J, Anangi R, Joshi RS, Giri AP, King GF, Barnwal RP, Chary KVR J Biomol Struct Dyn. 2019 Apr 30:1-10. doi: 10.1080/07391102.2019.1607559. PMID:31038412^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.