
LysM domain - Wikipedia
In molecular biology the LysM domain is a protein domain found in a wide variety of extracellular proteins and receptors. The LysM domain is named after the Lysin Motif which was the original name given to the sequence motif identified in bacterial proteins.
LysM, a widely distributed protein motif for binding to (peptido ...
Bacteria retain certain proteins at their cell envelopes by attaching them in a non-covalent manner to peptidoglycan, using specific protein domains, such as the prominent LysM (Lysin Motif) domain. More than 4000 (Pfam PF01476) proteins of both prokaryotes and eukaryotes have been found to contain …
Lysin Motif (LysM) Proteins: Interlinking Manipulation of Plant ...
The proteins with lysin motif (LysM) are carbohydrate-binding protein modules that play a critical role in the host-pathogen interactions. The plant LysM proteins mostly function as pattern recognition receptors (PRRs) that sense chitin to induce ...
CDD Conserved Protein Domain Family: LysM - National Center …
Oct 2, 2020 · LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain.
Exploiting the peptidoglycan-binding motif, LysM, for medical and ...
The lysin motif (LysM) was first identified by Garvey et al. in 1986 and, in subsequent studies, has been shown to bind noncovalently to peptidoglycan and chitin by interacting with N-acetylglucosamine moieties. The LysM sequence is present singly ...
LysM domain-containing proteins modulate stress response …
Sep 1, 2021 · Lysin-motif (LysM) and LysM receptor-like kinase (LYK) proteins play a major role in defence-response. The allohexaploid genome of Triticum aestivum consisted of 42 TaLysM and 20 TaLYK genes.
Plant LysM proteins: modules mediating symbiosis and immunity
Plant lysin motif (LysM) domain proteins serve as modules mediating recognition of these different N-acetylglucosamine (GlcNAc)-containing ligands, suggesting that this class of proteins evolved from an ancient sensor for GlcNAc.
Molecular basis for bacterial peptidoglycan recognition by LysM …
Jun 30, 2014 · LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall.
LysM proteins in mammalian fungal pathogens - ScienceDirect
Jun 1, 2022 · The LysM domain is a highly conserved carbohydrate-binding module that recognizes polysaccharides containing N-acetylglucosamine residues. LysM domains are found in a wide variety of extracellular proteins and receptors from …
How LysM binds to peptidoglycan - Nature Reviews Microbiology
Jul 16, 2014 · LysM is a highly conserved carbohydrate binding module that is present in proteins from all kingdoms, but how LysM binds its substrates is unknown. Mesnage et al. now show how a LysM domain...