4F0A
Crystal structure of XWnt8 in complex with the cysteine-rich domain of Frizzled 8
Summary for 4F0A
| Entry DOI | 10.2210/pdb4f0a/pdb |
| Related | 1IJY |
| Descriptor | Frizzled-8, Protein Wnt-8, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | wnt signaling, ligand-receptor complex, wnt, frizzled, fatty acid acylation, glycosylation, signaling protein |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Membrane; Multi-pass membrane protein: Q61091 Secreted, extracellular space, extracellular matrix: P28026 |
| Total number of polymer chains | 2 |
| Total formula weight | 52603.69 |
| Authors | Janda, C.Y.,Waghray, D.,Levin, A.M.,Thomas, C.,Garcia, K.C. (deposition date: 2012-05-03, release date: 2012-06-13, Last modification date: 2024-11-27) |
| Primary citation | Janda, C.Y.,Waghray, D.,Levin, A.M.,Thomas, C.,Garcia, K.C. Structural basis of Wnt recognition by Frizzled. Science, 337:59-64, 2012 Cited by PubMed Abstract: Wnts are lipid-modified morphogens that play critical roles in development principally through engagement of Frizzled receptors. The 3.25 angstrom structure of Xenopus Wnt8 (XWnt8) in complex with mouse Frizzled-8 (Fz8) cysteine-rich domain (CRD) reveals an unusual two-domain Wnt structure, not obviously related to known protein folds, resembling a "hand" with "thumb" and "index" fingers extended to grasp the Fz8-CRD at two distinct binding sites. One site is dominated by a palmitoleic acid lipid group projecting from serine 187 at the tip of Wnt's thumb into a deep groove in the Fz8-CRD. In the second binding site, the conserved tip of Wnt's "index finger" forms hydrophobic amino acid contacts with a depression on the opposite side of the Fz8-CRD. The conservation of amino acids in both interfaces appears to facilitate ligand-receptor cross-reactivity, which has important implications for understanding Wnt's functional pleiotropy and for developing Wnt-based drugs for cancer and regenerative medicine. PubMed: 22653731DOI: 10.1126/science.1222879 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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