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9SNT

Apo-form of Schistosoma mansoni Cathepsin D1 at 2.2A resolution

Summary for 9SNT
Entry DOI10.2210/pdb9snt/pdb
Related9RXI
DescriptorCathepsin D (A01 family) (2 entities in total)
Functional Keywordsapo-form, cathepsin d, lysosomal aspartyl protease, hydrolase
Biological sourceSchistosoma mansoni
Total number of polymer chains1
Total formula weight47001.06
Authors
Parker, K.,Clarke, J.D.,Liu, X.,Gomes, B.F.,Eyssen, L.E.,Furnham, N.,Silva-Jr, F.P.,Owens, R.J. (deposition date: 2025-09-11, release date: 2026-02-18)
Primary citationParker, K.L.,Clarke, J.D.,Liu, X.,Gomes, B.F.,Eyssen, L.E.A.,Furnham, N.,Paes Silva-Jr, F.,Owens, R.J.
Crystal structure of Schistosoma mansoni cathepsin D1 in complex with a nanobody reveals the conformation of the propeptide-bound state.
Acta Crystallogr D Struct Biol, 82:140-150, 2026
Cited by
PubMed Abstract: Schistosoma mansoni cathepsin D1 (SmCD1) has been shown to be an essential enzyme for helminth metabolism due to its role in haemoglobin degradation: a key amino-acid source for the developing parasite. Therefore, the enzyme is a potential target for the development of antischistosomal inhibitors. SmCD1 has significant sequence identity to cathepsin D-like proteases found in other schistosome species and homology to mammalian aspartic proteases. Here, we report the first crystal structures of a helminth cathepsin D, SmCD1, and have identified a single-domain antibody (nanobody) that specifically binds to SmCD1 with nanomolar affinity but does not recognize human cathepsin D. We have mapped the epitope of the nanobody by determining the crystal structure of the enzyme-nanobody complex, revealing the conformation of SmCD1 in the propeptide-bound state.
PubMed: 41603320
DOI: 10.1107/S2059798326000422
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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PDB entries from 2026-03-11

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