Member database | Pfam |
Pfam type | domain |
Short name | DIKK1-2-4_C-subdom2 |
Clan | Colipase |
Author | Bateman A;0000-0002-6982-4660 Chuguransky S;0000-0002-0520-0736 |
Sequence Ontology | 0000417 |
Description
Dickkopf-related proteins are cysteine-rich secretory proteins and highly conserved inhibitors of the canonical Wnt signaling pathway, which play key roles in many essential biological processes. The C-terminal domain is described as two subdomains, each consisting of three anti-parallel beta-strands that are connected by a long loop which contains a short alpha-helix. This domain is strongly conserved in Dkk1, Dkk2 and Dkk4, and directly contacts LRP6. This entry represents the second subdomain [1-4]. In Dkk3 these residues differ and is consistent with studies indicating that Dkk3 is a divergent family member that does not inhibit Wnt signalling
[1]. This domain share significant sequence similarity to the colipase fold.
References
Further reading
2. Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6. Ahn VE, Chu ML, Choi HJ, Tran D, Abo A, Weis WI. Dev Cell 21, 862-73, (2011). PMID: 22000856
3. Crystal structures of the extracellular domain of LRP6 and its complex with DKK1. Cheng Z, Biechele T, Wei Z, Morrone S, Moon RT, Wang L, Xu W. Nat Struct Mol Biol 18, 1204-10, (2011). View articlePMID: 21984209
4. Structural insight into the mechanisms of Wnt signaling antagonism by Dkk. Chen L, Wang K, Shao Y, Huang J, Li X, Shan J, Wu D, Zheng JJ. J. Biol. Chem. 283, 23364-70, (2008). View articlePMID: 18524778