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Titolo:
COMPARATIVE MODELING OF BARLEY-GRAIN ASPARTIC PROTEINASE - A STRUCTURAL RATIONALE FOR OBSERVED HYDROLYTIC SPECIFICITY
Autore:
GURUPRASAD K; TORMAKANGAS K; KERVINEN J; BLUNDELL TL;
Indirizzi:
UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,MOLEC BIOL LAB,MALET ST LONDON WC1E 7HX ENGLAND UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,MOLEC BIOL LAB LONDON WC1E 7HX ENGLAND UNIV HELSINKI,INST BIOTECHNOL SF-00014 HELSINKI FINLAND
Titolo Testata:
FEBS letters
fascicolo: 2, volume: 352, anno: 1994,
pagine: 131 - 136
SICI:
0014-5793(1994)352:2<131:CMOBAP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY ANALYSES; ACID SUBSTITUTION TABLES; HUMAN CATHEPSIN-D; SECONDARY STRUCTURE; HOMOLOGOUS PROTEINS; DATA-BANK; PREDICTION; TEMPLATES; DESIGN; RESOLUTION;
Keywords:
HORDEUM VULGARE; BARLEY GRAIN; ASPARTIC PROTEINASE; HYDROLYTIC SPECIFICITY; PROTEIN STRUCTURE PREDICTION; SPECIFICITY POCKET;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
K. Guruprasad et al., "COMPARATIVE MODELING OF BARLEY-GRAIN ASPARTIC PROTEINASE - A STRUCTURAL RATIONALE FOR OBSERVED HYDROLYTIC SPECIFICITY", FEBS letters, 352(2), 1994, pp. 131-136

Abstract

A model of the barley-grain aspartic proteinase (HvAP; Hordeum vulgare aspartic proteinase) has been constructed using the rule-based comparative modelling approach encoded in the COMPOSER suite of computer programs. The model was based on the high resolution crystal structures of six highly homologous aspartic proteinases. Results suggest that the overall three-dimensional structure of HvAP (excluding the plant-specific insert; 104 residues in HvAP) is closer to human cathepsin D than other aspartic proteinases of known three-dimensional structure. Comparisons of the complexes with the substrate modelled in the active site of HvAP with those of the same substrate modelled in the active site of other aspartic proteinases of known three-dimensional structure and specificity, define residues that may influence hydrolytic specificity of the barley enzyme. We have identified residues in the S-4 (Ala(12)), S-3 (Gln(13), Thr(111)), S-2 (Ala(222), Thr(287), Met(289)), S-1' and S-3' (Ile(291)), S-2' and S-3' (Gln(74)), S-2' (Arg(295)), and S-3' (Pro(292)) pockets, that may account for the observed trends in the kinetic behaviour and specificity when compared to other aspartic proteinases. The plant-specific inserted sequence, which may play a rolein the transport of HvAP to plant vacuoles (lysosomes), is similar tothe saposins and is predicted to be a mixed alpha-helical and beta-strand domain.

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Documento generato il 01/12/20 alle ore 07:46:03