Abstract:
:A series of secreted proteases are included among the virulence factors documented for Staphylococcus aureus. In light of increasing antibiotic resistance of this dangerous human pathogen, these proteases are considered as suitable targets for the development of novel therapeutic strategies. The recent discovery of staphostatins, endogenous, highly specific, staphylococcal cysteine protease inhibitors, opened a possibility for structure-based design of low molecular weight analogues. Moreover, the crystal structure of staphostatin B revealed a distinct folding pattern and an unexpected, substrate-like binding mode. The solution structure of staphostatin A reported here confirms that staphostatins constitute a novel, distinct class of cysteine protease inhibitors. In addition, the structure knowledge-based mutagenesis studies shed light on individual structural features of staphostatin A, the inhibition mechanism, and the determinants of distinct specificity of staphostatins toward their target proteases.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Dubin G,Krajewski M,Popowicz G,Stec-Niemczyk J,Bochtler M,Potempa J,Dubin A,Holak TAdoi
10.1021/bi035310jsubject
Has Abstractpub_date
2003-11-25 00:00:00pages
13449-56issue
46eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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