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3WSY

SorLA Vps10p domain in complex with its own propeptide fragment

Summary for 3WSY
Entry DOI10.2210/pdb3wsy/pdb
Related3WSX 3WSZ
DescriptorSortilin-related receptor, peptide from Sortilin-related receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsbeta-propeller, receptor, protein binding
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight79373.73
Authors
Kitago, Y.,Nakata, Z.,Nagae, M.,Nogi, T.,Takagi, J. (deposition date: 2014-03-30, release date: 2015-02-04, Last modification date: 2024-10-30)
Primary citationKitago, 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: 25643321
DOI: 10.1038/nsmb.2954
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.11 Å)
Structure validation

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