2J0A
Structure of the catalytic domain of mouse Manic Fringe
Summary for 2J0A
| Entry DOI | 10.2210/pdb2j0a/pdb |
| Related | 2J0B |
| Descriptor | BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE MANIC FRINGE, SULFATE ION, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | glycosyltransferase, developmental protein, transmembrane, golgi apparatus, notch signaling, membrane, transferase, glycoprotein, signal-anchor |
| Biological source | MUS MUSCULUS (MOUSE) |
| Cellular location | Golgi apparatus membrane; Single-pass type II membrane protein (By similarity): O09008 |
| Total number of polymer chains | 1 |
| Total formula weight | 31684.45 |
| Authors | Jinek, M.,Chen, Y.-W.,Clausen, H.,Cohen, S.M.,Conti, E. (deposition date: 2006-08-01, release date: 2006-09-04, Last modification date: 2024-11-20) |
| Primary citation | Jinek, M.,Chen, Y.-W.,Clausen, H.,Cohen, S.M.,Conti, E. Structural Insights Into the Notch-Modifying Glycosyltransferase Fringe Nat.Struct.Mol.Biol., 13:945-, 2006 Cited by PubMed Abstract: Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo. PubMed: 16964258DOI: 10.1038/NSMB1144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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