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Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors.
Protein Sci. 2002 Aug; 11(8):1971-7.PS

Abstract

The recently described inhibitor of cysteine proteinases from Trypanosoma cruzi, chagasin, was found to have close homologs in several eukaryotes, bacteria and archaea, the first protein inhibitors of cysteine proteases in prokaryotes. These previously uncharacterized 110-130 residue-long proteins share a well-conserved sequence motif that corresponds to two adjacent beta-strands and the short loop connecting them. Chagasin-like proteins also have other conserved, mostly aromatic, residues, and share the same predicted secondary structure. These proteins adopt an all-beta fold with eight predicted beta-strands of the immunoglobulin type. The phylogenetic distribution of the chagasins generally correlates with the presence of papain-like cysteine proteases. Previous studies have uncovered similar trends in cysteine proteinase binding by two unrelated inhibitors, stefin and p41, that belong to the cystatin and thyroglobulin families, respectively. A hypothetical model of chagasin-cruzipain interaction suggests that chagasin may dock to the cruzipain active site in a similar manner with the conserved NPTTG motif of chagasin forming a loop that is similar to the wedge structures formed at the active sites of papain and cathepsin L by stefin and p41.

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Authors+Show Affiliations

Rigden DJ
National Centre of Genetic Resources and Biotechnology, Cenargen/Embrapa, S.A.I.N. Parque Rural, Final W5 Norte, 70770-900 Brasília, Brazil. daniel@cenargen.embrapa.br
Mosolov VV
No affiliation info available
Galperin MY
No affiliation info available

MeSH

Amino Acid SequenceBinding SitesConserved SequenceCysteine EndopeptidasesCysteine Proteinase InhibitorsDatabases, ProteinModels, MolecularMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryProtozoan ProteinsSequence AlignmentSequence Homology, Amino Acid

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12142451

Citation

Rigden, Daniel J., et al. "Sequence Conservation in the Chagasin Family Suggests a Common Trend in Cysteine Proteinase Binding By Unrelated Protein Inhibitors." Protein Science : a Publication of the Protein Society, vol. 11, no. 8, 2002, pp. 1971-7.
Rigden DJ, Mosolov VV, Galperin MY. Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors. Protein Sci. 2002;11(8):1971-7.
Rigden, D. J., Mosolov, V. V., & Galperin, M. Y. (2002). Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors. Protein Science : a Publication of the Protein Society, 11(8), 1971-7.
Rigden DJ, Mosolov VV, Galperin MY. Sequence Conservation in the Chagasin Family Suggests a Common Trend in Cysteine Proteinase Binding By Unrelated Protein Inhibitors. Protein Sci. 2002;11(8):1971-7. PubMed PMID: 12142451.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors. AU - Rigden,Daniel J, AU - Mosolov,Vladimir V, AU - Galperin,Michael Y, PY - 2002/7/27/pubmed PY - 2002/12/21/medline PY - 2002/7/27/entrez SP - 1971 EP - 7 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 11 IS - 8 N2 - The recently described inhibitor of cysteine proteinases from Trypanosoma cruzi, chagasin, was found to have close homologs in several eukaryotes, bacteria and archaea, the first protein inhibitors of cysteine proteases in prokaryotes. These previously uncharacterized 110-130 residue-long proteins share a well-conserved sequence motif that corresponds to two adjacent beta-strands and the short loop connecting them. Chagasin-like proteins also have other conserved, mostly aromatic, residues, and share the same predicted secondary structure. These proteins adopt an all-beta fold with eight predicted beta-strands of the immunoglobulin type. The phylogenetic distribution of the chagasins generally correlates with the presence of papain-like cysteine proteases. Previous studies have uncovered similar trends in cysteine proteinase binding by two unrelated inhibitors, stefin and p41, that belong to the cystatin and thyroglobulin families, respectively. A hypothetical model of chagasin-cruzipain interaction suggests that chagasin may dock to the cruzipain active site in a similar manner with the conserved NPTTG motif of chagasin forming a loop that is similar to the wedge structures formed at the active sites of papain and cathepsin L by stefin and p41. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/12142451/Sequence_conservation_in_the_chagasin_family_suggests_a_common_trend_in_cysteine_proteinase_binding_by_unrelated_protein_inhibitors_ DB - PRIME DP - Unbound Medicine ER -