9D3Y

Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Compound S2

This is a non-PDB format compatible entry.

Summary for 9D3Y

• Entry DOI: 10.2210/pdb9d3y/pdb
• Related: 9D17
• Descriptor: Mannan-binding lectin serine protease 2 B chain, GLYCEROL, (2S)-N-[2-(2-amino-1H-1,3-benzimidazol-5-yl)ethyl]-1-[(2R,4S)-4-phenylpiperidine-2-carbonyl]azetidine-2-carboxamide, ... (4 entities in total)
• Functional Keywords: inhibitor, masp2, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 36364.96

Authors

Sawyer, T.K.,Wibowo, A.S.,Carter, J.,Moussa, S.H. (deposition date: 2024-08-12, release date: 2025-04-16)

Primary citation

Nakhla, M.C.,Comita, J.,Shapiro, A.B.,Moussa, S.H.,Chen, A.,Eyermann, C.J.,O'Donnell, J.P.,Miller, A.A.,Granger, B.A.
Small molecule inhibitors of mannan-binding lectin-associated serine Proteases-2 and-3.
Eur.J.Med.Chem., 289:117238-117238, 2025

PubMed Abstract: The complement system of innate immunity recognizes, opsonizes, and kills invading pathogens and damaged cells, and stimulates an inflammatory response. Inappropriate or excessive complement activity is associated with a wide variety of pathological conditions, and several drugs targeting complement components have been approved. Here we describe the discovery and structure-activity relationships of a novel class of 2-aminoimidazole-containing inhibitors of mannan-binding lectin-associated serine proteases -2 and -3 (MASP-2 and MASP-3), essential enzymes for activation of the lectin and alternative pathways of complement, respectively. With a high degree of target selectivity and favorable in vitro pharmacological properties, this inhibitor series has the potential to be developed as treatments for numerous diseases and pathological conditions.

PubMed: 40010268
DOI: 10.1016/j.ejmech.2025.117238

Experimental method

X-RAY DIFFRACTION (2.08 Å)