1oh1: Difference between revisions

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[[Image:1oh1.jpg|left|200px]]<br /><applet load="1oh1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1oh1.jpg|left|200px]]<br /><applet load="1oh1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1oh1" />

'''SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.'''<br />

==Overview==

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.

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 Structure==

1OH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1OH1 OCA].

1OH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OH1 OCA].

==Reference==

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[[Category: staphopain inhibitor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1oh1.jpg|left|200px]]<br /><applet load="1oh1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1oh1.jpg|left|200px]]<br /><applet load="1oh1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1oh1" />
 '''SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.'''<br />
 ==Overview==
-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.
+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 Structure==
-OH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OH1 OCA].
+OH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OH1 OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: staphopain inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:54:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:38 2008''