Kasuya, A; Thornton, JM; (1999) Three-dimensional structure analysis of PROSITE patterns. Journal of Molecular Biology , 286 (5) 1673 - 1691.
Full text not available from this repository.
Pattern matches for each of the sequence patterns in PROSITE, a database of sequence patterns, were searched in all protein sequences in the Brookhaven Protein Data Bank (PDB). The three-dimensional structures of the pattern matches for the 20 patterns with the largest numbers of hits were analysed. We found that the true positives have a common three-dimensional structure for each pattern; the structures of false positives, found for six of the 20 patterns, were clearly different from those of the true positives. The results suggest that the true pattern matches each have a characteristic common three- dimensional structure, which could be used to create a template to define a three-dimensional functional pattern. Copyright 1998 Academic Press
|Title:||Three-dimensional structure analysis of PROSITE patterns|
|Additional information:||UI - 99165794 LA - Eng RN - EC 1.11.1. (Peroxidases) RN - EC 126.96.36.199 (Trypsin) RN - EC 3.4.23 (Aspartic Endopeptidases) RN -EC 188.8.131.52 (RNA Ligase (ATP)) RN - 0 (Annexins) RN - 0 (Proteins) RN - 56-65-5 (Adenosine Triphosphate) RN - 7440-50-8 (Copper) RN -86-01-1 (Guanosine Triphosphate) RN - 9007-43-6 (Cytochrome c) PT - JOURNAL ARTICLE DA - 19990427 IS - 0022-2836 SB - M SB - X CY -ENGLAND JC - J6V AA - Author EM - 199907|
|Keywords:||Structure, analysis, Trypsin, ATP, Proteins, Adenosine, Adenosine Triphosphate, Copper, Cytochrome c, Amino Acid Sequence, Annexins, Aspartic Endopeptidases, Biochemistry, chemistry, classification, Comparative Study, Conserved Sequence, database, Databases, Factual, False Positive Reactions, Guanosine Triphosphate, metabolism, Models, Molecular, Molecular Biology, Pattern Recognition, Peroxidases, Protein Conformation, RNA Ligase (ATP), Structure-Activity Relationship, Support, Non-U.S.Gov't|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
Archive Staff Only: edit this record