|PROSITE documentation PDOC51051 [for PROSITE entry PS51051]|
The about 50 amino acids DSL (Delta / Serrate / Lag-2) domain is an extracellular domain essential to activate members of the Lin-12/Notch receptors family. The DSL domain may mediates oligomerization of DSL proteins to form an active ligand and mediates interaction with the extracellular domain of Lin-12/Notch proteins involved in cell-cell signaling interactions [1,2,3]. The DSL domain is found followed by a variable number of tandemly repeated copies of EGF motifs (see <PDOC00021>). Like EGF motifs this domain contains six conserved cysteines spanning different sequence lengths. Furthermore, the DSL domain contains a conserved YYG motif not present in the EGF motifs.
The DSL domain has clear structural similarities to an EGF domain, with a double-stranded antiparallel β-sheet immediately preceding the characteristic loop between the final disulfide-bonded cysteines residues (see <PDB:2VJ2>). However, the DSL domain adopts a fold with a different disulfide-bonded pattern (C1-C2, C3-C4, C5-C6). On the basis of the structure, it has been proposed that the DSL domain may have evolved from a truncation of two tandem short EGF domains .
Proteins currently known to contain a DSL domain are:
The profile we developed covers the entire DSL domain.Last update:
November 2011 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Artavanis-Tsakonas S. Matsuno K. Fortini M.E.|
|2||Authors||Fitzgerald K. Greenwald I.|
|Title||Interchangeability of Caenorhabditis elegans DSL proteins and intrinsic signalling activity of their extracellular domains in vivo.|
|3||Authors||Henderson S.T. Gao D. Lambie E.J. Kimble J.|
|Title||lag-2 may encode a signaling ligand for the GLP-1 and LIN-12 receptors of C. elegans.|
|4||Authors||Cordle J. Johnson S. Tay J.Z.Y. Roversi P. Wilkin M.B. Hernandez de Madrid B. Shimizu H. Jensen S. Whiteman P. Jin B. Redfield C. Baron M. Lea S.M. Handford P.A.|
|Title||A conserved face of the Jagged/Serrate DSL domain is involved in Notch trans-activation and cis-inhibition.|
|Source||Nat. Struct. Mol. Biol. 15:849-857(2008).|
|5||Authors||Yuan Z.R. Okaniwa M. Nagata I. Tazawa Y. Ito M. Kawarazaki H. Inomata Y. Okano S. Yoshida T. Kobayashi N. Kohsaka T.|
|Title||The DSL domain in mutant JAG1 ligand is essential for the severity of the liver defect in Alagille syndrome.|
|Source||Clin. Genet. 59:330-337(2001).|