LysMs are a family of carbohydrate-binding modules with a length of approximately 50 amino acids and bind to N-acetylglucosamine (GlcNAc -containing GlcNAc -containinghitin, chitin-like compounds and peptidoglycans(Buisucht as. 2008).
Individual domains frequently act as discrete ligand-binding modules, with a diverse set of host endothelial surface proteins and carbohydrates identified as partners for different domains (Smith et al., 2013).
R. albus 7 has 35 proteins predicted to contain binding modules with no adjacent catalytic domains, including 26 containing a single CBM37, 8 that each contain 2 CBM37 domains, 1 that contains a CBM37 and a CBM2 domain, 1 that contains 2 CBM37 domains, and 2 containing a CBM13 and a CBM37 domains.
Further analysis of domain architecture reveals the association of carbohydrate binding modules with catalytic GH β-helices, as well as an unexpected pair of β-helix domains in GH family 55.
We propose this to comprise a potential site for interaction of the effector-binding module with a specific DNA-binding domain, so as to mimic the organisation of the multi-domain transcription regulators.
It is also worth noting that, like Cel7B, GH10 EX has a cellulose binding module with high affinity to cellulose [ 42, 43].
Combining endoglucanase and cellobiohydrolase activity along with carbohydrate binding modules in a single molecule may ensure proximity of these complementary catalytic domains, and therefore enhanced activity, while also preventing diffusion of these proteins away from their insoluble substrates.
Cancer imaging requires small, fast penetrating but tightly binding targeting modules, with a rapid plasma clearance.
The binding of modified H. insolens EGV and T. reesei CBHI, i.e. these enyzmes without the cellulose binding module or with an inactive catalytic domain, were also investigated.
Only 12 P. parasitica CWDEs contain both catalytically-active (glycosyl hydrolase) and non-catalytic (carbohydrate binding) modules, a situation that contrasts with that in fungal phytopathogens.
We have re-examined the role of the 53BP1-BRCT2 domand and show unambiguously that it is a competent binding module for phosphorylated peptides with a clear specificity for the DNA-damage marker γH2AX, and in isolation from other parts of 53BP1 is sufficient for localization to sites of DNA damage in cells associated with γH2AX.
