Crystal structure of LRP6 E3E4 in complex with disulfide constrained peptide E3.18. Determined by X-ray diffraction at 2.5 Å resolution. Released 29 Mar 2023.
Explore 8DVL in 3D Show helices and sheets RCSB PDB PDBe
8DVL contains 7 α-helices and 58 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 633-638 | 6 | 1 |
| β-strand | 641-646 | 6 | 1 |
| β-strand | 653-655 | 3 | 1 |
| β-strand | 664-670 | 7 | 2 |
| β-strand | 675-680 | 6 | 2 |
| β-strand | 685-690 | 6 | 2 |
| β-strand | 697-700 | 4 | 2 |
| β-strand | 709-713 | 5 | 3 |
| β-strand | 718-723 | 6 | 3 |
| β-strand | 728-733 | 6 | 3 |
| β-strand | 740-743 | 4 | 3 |
| β-strand | 750-756 | 7 | 4 |
| β-strand | 761-766 | 6 | 4 |
| β-strand | 772-777 | 6 | 4 |
| β-strand | 784-787 | 4 | 4 |
| β-strand | 793-799 | 7 | 5 |
| β-strand | 804-809 | 6 | 5 |
| β-strand | 814-819 | 6 | 5 |
| β-strand | 826-829 | 4 | 5 |
| β-strand | 835-841 | 7 | 6 |
| β-strand | 844-849 | 6 | 6 |
| β-strand | 854-859 | 6 | 6 |
| β-strand | 867-870 | 4 | 6 |
| β-strand | 876-882 | 7 | 1 |
| α-helix | 884-886 | 3 | |
| α-helix | 892-896 | 5 | |
| α-helix | 897-899 | 3 | |
| β-strand | 903-906 | 4 | 7 |
| β-strand | 912-915 | 4 | 7 |
| β-strand | 921-922 | 2 | 8 |
| β-strand | 929-930 | 2 | 8 |
| β-strand | 935-940 | 6 | 9 |
| β-strand | 943-947 | 5 | 9 |
| β-strand | 957-958 | 2 | 9 |
| β-strand | 967-973 | 7 | 10 |
| β-strand | 978-983 | 6 | 10 |
| β-strand | 988-992 | 5 | 10 |
| β-strand | 1000-1003 | 4 | 10 |
| β-strand | 1016-1022 | 7 | 11 |
| β-strand | 1027-1032 | 6 | 11 |
| β-strand | 1037-1042 | 6 | 11 |
| β-strand | 1047-1053 | 7 | 11 |
| β-strand | 1059-1065 | 7 | 12 |
| β-strand | 1070-1077 | 8 | 12 |
| β-strand | 1080-1087 | 8 | 12 |
| β-strand | 1094-1097 | 4 | 12 |
| β-strand | 1104-1110 | 7 | 13 |
| β-strand | 1115-1120 | 6 | 13 |
| β-strand | 1125-1130 | 6 | 13 |
| β-strand | 1137-1140 | 4 | 13 |
| β-strand | 1147-1153 | 7 | 14 |
| β-strand | 1156-1161 | 6 | 14 |
| β-strand | 1166-1171 | 6 | 14 |
| α-helix | 1177-1178 | 2 | |
| β-strand | 1179-1182 | 4 | 14 |
| β-strand | 1188-1194 | 7 | 9 |
| α-helix | 1195-1197 | 3 | |
| α-helix | 1199-1203 | 5 | |
| α-helix | 1210-1213 | 4 | |
| β-strand | 1217-1220 | 4 | 15 |
| β-strand | 1226-1229 | 4 | 15 |
| β-strand | 1235-1236 | 2 | 16 |
| β-strand | 1243-1244 | 2 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 17 |
| β-strand | 10-13 | 4 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Low-density lipoprotein receptor-related protein 6 | A | protein | 633 | Homo sapiens | O75581 (AlphaFold model) |
| E3.18 Disulfide constrained peptide | B | protein | 32 | synthetic construct |
>8DVL_1 Low-density lipoprotein receptor-related protein 6 (chains A) SEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRA FMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDS PRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTD LDTNLIESSNMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTII QGHLDYVMDILVFHSSRQSGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTC SAPTTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNMI RKAQEDGSQGFTVVVSSVPSQNLEIQPYDLSIDIYSRYIYWTCEATNVINVTRLDGRSVG VVLKGEQDRPRAIVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALAL DSRLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEK IDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCS CPMHLVLLQDELSCGEPPTCSPQQGNSHHHHHH
>8DVL_2 E3.18 Disulfide constrained peptide (chains B) GCIPVITTRGVRCKQDSDCLAGCVCDVSQACG
Water and common crystallization additives (EDO) are not listed.
Synthetic Multivalent Disulfide-Constrained Peptide Agonists Potentiate Wnt1/ beta-Catenin Signaling via LRP6 Coreceptor Clustering. Thakur, A.K., Miller, S.E., Liau, N.P.D. et al. ACS Chem Biol (2023) 18:772-784. DOI 10.1021/acschembio.2c00753 · PubMed
Other PDB entries of the same protein (UniProt O75581 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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