5mwf

Human Jagged2 C2-EGF2

spinqualitylabelsall models 5mwf, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mwf is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: BMA, CA, CL, FUC, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function JAG2_HUMAN Putative Notch ligand involved in the mediation of Notch signaling. Involved in limb development (By similarity). Publication Abstract from PubMed Recent data have expanded our understanding of Notch signalling by identifying a C2 domain at the N-terminus of Notch ligands, which has both lipid- and receptor-binding properties. We present novel structures of human ligands Jagged2 and Delta-like4 and human Notch2, together with functional assays, which suggest that ligand-mediated coupling of membrane recognition and Notch binding is likely to be critical in establishing the optimal context for Notch signalling. Comparisons between the Jagged and Delta family show a huge diversity in the structures of the loops at the apex of the C2 domain implicated in membrane recognition and Jagged1 missense mutations, which affect these loops and are associated with extrahepatic biliary atresia, lead to a loss of membrane recognition, but do not alter Notch binding. Taken together, these data suggest that C2 domain binding to membranes is an important element in tuning ligand-dependent Notch signalling in different physiological contexts. Structural and functional dissection of the interplay between lipid and Notch binding by human Notch ligands.,Suckling RJ, Korona B, Whiteman P, Chillakuri C, Holt L, Handford PA, Lea SM EMBO J. 2017 Aug 1;36(15):2204-2215. doi: 10.15252/embj.201796632. Epub 2017 Jun , 1. PMID:28572448 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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