Thimet oligopeptidase and neurolysin are closely related zinc-dependent metallopeptidases that metabolize small bioactive peptides. They cleave many substrates at the same sites, but they recognise different positions on others. This entry represents the up-down alpha bundle domain found at the N terminus of these and related M3 peptidases. Paper describing PDB structure 1i1i. [1]. 11248043. Structure of neurolysin reveals a deep channel that limits substrate access. Brown CK, Madauss K, Lian W, Beck MR, Tolbert WD, Rodgers DW;. Proc Natl Acad Sci U S A. 2001;98:3127-3132. Paper describing PDB structure 1s4b. [2]. 14998993. Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization. Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW;. J Biol Chem. 2004;279:20480-20489. Paper describing PDB structure 1y79. [3]. 15876371. Crystal structure of the E. coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependent hinge movement mechanism. Comellas-Bigler M, Lang R, Bode W, Maskos K;. J Mol Biol. 2005;349:99-112. Paper describing PDB structure 2o36. [4]. 17251185. Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase. Lim EJ, Sampath S, Coll-Rodriguez J, Schmidt J, Ray K, Rodgers DW;. J Biol Chem. 2007;282:9722-9732. Paper describing PDB structure 4fxy. [5]. 25378390. Allosteric inhibition of the neuropeptidase neurolysin. Hines CS, Ray K, Schmidt JJ, Xiong F, Feenstra RW, Pras-Raves M, de Moes JP, Lange JH, Melikishvili M, Fried MG, Mortenson P, Charlton M, Patel Y, Courtney SM, Kruse CG, Rodgers DW;. J Biol C. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16