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Proteases universally recognize beta strands in their active sites.

Author(s): Joel Tyndall, W D Fairlie, B T Nall

Publication date: 2005-02-28

Journal: Chemical Reviews

Keywords: Animals, Aspartic Acid Endopeptidases, chemistry, metabolism, Binding Sites, Cysteine Endopeptidases, Humans, Metalloproteases, Peptide Hydrolases, Protease Inhibitors, Protein Structure, Secondary, Serine Endopeptidases, Structure-Activity Relationship, Substrate Specificity

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PubMed ID:: 15755082

DOI:: 10.1021/cr040669e

ScienceOpen disciplines: Chemistry

Keywords: Animals,Aspartic Acid Endopeptidases,chemistry,metabolism,Binding Sites,Cysteine Endopeptidases,Humans,Metalloproteases,Peptide Hydrolases,Protease Inhibitors,Protein Structure, Secondary,Serine Endopeptidases,Structure-Activity Relationship,Substrate Specificity

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ScienceOpen disciplines: Chemistry

Keywords: Animals, Aspartic Acid Endopeptidases, chemistry, metabolism, Binding Sites, Cysteine Endopeptidases, Humans, Metalloproteases, Peptide Hydrolases, Protease Inhibitors, Protein Structure, Secondary, Serine Endopeptidases, Structure-Activity Relationship, Substrate Specificity

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