3WSX
SorLA Vps10p domain in ligand-free form
Summary for 3WSX
| Entry DOI | 10.2210/pdb3wsx/pdb |
| Related | 3WSY 3WSZ |
| Descriptor | Sortilin-related receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | beta-propeller, receptor, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 84255.88 |
| Authors | Kitago, Y.,Nakata, Z.,Nagae, M.,Nogi, T.,Takagi, J. (deposition date: 2014-03-30, release date: 2015-02-04, Last modification date: 2024-11-20) |
| Primary citation | Kitago, Y.,Nagae, M.,Nakata, Z.,Yagi-Utsumi, M.,Takagi-Niidome, S.,Mihara, E.,Nogi, T.,Kato, K.,Takagi, J. Structural basis for amyloidogenic peptide recognition by sorLA. Nat.Struct.Mol.Biol., 22:199-206, 2015 Cited by PubMed Abstract: SorLA is a neuronal sorting receptor considered to be a major risk factor for Alzheimer's disease. We have recently reported that it directs lysosomal targeting of nascent neurotoxic amyloid-β (Aβ) peptides by directly binding Aβ. Here, we determined the crystal structure of the human sorLA domain responsible for Aβ capture, Vps10p, in an unbound state and in complex with two ligands. Vps10p assumes a ten-bladed β-propeller fold with a large tunnel at the center. An internal ligand derived from the sorLA propeptide bound inside the tunnel to extend the β-sheet of one of the propeller blades. The structure of the sorLA Vps10p-Aβ complex revealed that the same site is used. Peptides are recognized by sorLA Vps10p in redundant modes without strict dependence on a particular amino acid sequence, thus suggesting a broad specificity toward peptides with a propensity for β-sheet formation. PubMed: 25643321DOI: 10.1038/nsmb.2954 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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