Difference between revisions of "LysM domain"
(→B. subtilis proteins containing a LysM domain) |
(→B. subtilis proteins containing a LysM domain) |
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* [[YocH]] | * [[YocH]] | ||
* [[YqfZ]] | * [[YqfZ]] | ||
| + | --- | ||
| + | * [[SpoVID]] | ||
| + | * [[YpbE]] | ||
| + | * [[YqbP]] | ||
| + | * [[YueA]] | ||
== Related SubtiWiki pages == | == Related SubtiWiki pages == | ||
Revision as of 08:56, 4 May 2016
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
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Related SubtiWiki pages
Important reviews
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)
