Difference between revisions of "LysM domain"
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* [[XlyB]] | * [[XlyB]] | ||
* [[YaaH]] | * [[YaaH]] | ||
| − | * [[YdhD] | + | * [[YdhD]] |
* [[YkvP]] | * [[YkvP]] | ||
* [[YkzQ]] | * [[YkzQ]] | ||
Revision as of 15:12, 27 December 2013
Contents
- 1 LysM domains have affinity for N-acetylglucosamine polymers (GlcNac) in the lower μM range. A single LysM domain is able to bind carbohydrate ligands and LysM domains act additively to increase the binding-affinity.
- 2 B. subtilis proteins containing a LysM domain
- 3 Related SubtiWiki pages
- 4 Important reviews
- 5 Important original publications
- 6 Back to Domains
LysM domains have affinity for N-acetylglucosamine polymers (GlcNac) in the lower μM range. A single LysM domain is able to bind carbohydrate ligands and LysM domains act additively to increase the binding-affinity.
B. subtilis proteins containing a LysM domain
Related SubtiWiki pages
Important reviews
Girbe Buist, Anton Steen, Jan Kok, Oscar P Kuipers
LysM, a widely distributed protein motif for binding to (peptido)glycans.
Mol Microbiol: 2008, 68(4);838-47
[PubMed:18430080]
[WorldCat.org]
[DOI]
(I p)
Important original publications
Jaslyn E M M Wong, Husam M A B Alsarraf, Jørn Døvling Kaspersen, Jan Skov Pedersen, Jens Stougaard, Søren Thirup, Mickaël Blaise
Cooperative binding of LysM domains determines the carbohydrate affinity of a bacterial endopeptidase protein.
FEBS J: 2014, 281(4);1196-208
[PubMed:24355088]
[WorldCat.org]
[DOI]
(I p)
