1oh1: Difference between revisions

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[[Image:1oh1.jpg|left|200px]]
[[Image:1oh1.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oh1 OCA], [http://www.ebi.ac.uk/pdbsum/1oh1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oh1 RCSB]</span>
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'''SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.'''
'''SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.'''
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[[Category: Potempa, J.]]
[[Category: Potempa, J.]]
[[Category: Stec, J.]]
[[Category: Stec, J.]]
[[Category: cysteine protease inhibitor]]
[[Category: Cysteine protease inhibitor]]
[[Category: not similar to cystatin]]
[[Category: Not similar to cystatin]]
[[Category: staphopain inhibitor]]
[[Category: Staphopain inhibitor]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:15 2008''

Revision as of 03:50, 3 May 2008

File:1oh1.jpg

Template:STRUCTURE 1oh1

SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.


OverviewOverview

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.

About this StructureAbout this Structure

1OH1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus., Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA, Biochemistry. 2003 Nov 25;42(46):13449-56. PMID:14621990 Page seeded by OCA on Sat May 3 03:50:11 2008

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