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Structural Catalytic Core of the Members of the Superfamily of Acid Proteases.
Denesyuk, Alexander I; Denessiouk, Konstantin; Johnson, Mark S; Uversky, Vladimir N.
Afiliación
  • Denesyuk AI; Structural Bioinformatics Laboratory, Biochemistry, InFLAMES Research Flagship Center, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.
  • Denessiouk K; Structural Bioinformatics Laboratory, Biochemistry, InFLAMES Research Flagship Center, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.
  • Johnson MS; Structural Bioinformatics Laboratory, Biochemistry, InFLAMES Research Flagship Center, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.
  • Uversky VN; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.
Molecules ; 29(15)2024 Jul 23.
Article en En | MEDLINE | ID: mdl-39124857
ABSTRACT
The superfamily of acid proteases has two catalytic aspartates for proteolysis of their peptide substrates. Here, we show a minimal structural scaffold, the structural catalytic core (SCC), which is conserved within each family of acid proteases, but varies between families, and thus can serve as a structural marker of four individual protease families. The SCC is a dimer of several structural blocks, such as the DD-link, D-loop, and G-loop, around two catalytic aspartates in each protease subunit or an individual chain. A dimer made of two (D-loop + DD-link) structural elements makes a DD-zone, and the D-loop + G-loop combination makes a psi-loop. These structural markers are useful for protein comparison, structure identification, protein family separation, and protein engineering.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Dominio Catalítico Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Finlandia Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Modelos Moleculares / Dominio Catalítico Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Finlandia Pais de publicación: Suiza