1nyc: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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-[[Image:1nyc.jpg|left|200px]]
+{{Seed}}
+[[Image:1nyc.png|left|200px]]
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 {{STRUCTURE_1nyc|  PDB=1nyc  |  SCENE=  }}
-'''Staphostatins resemble lipocalins, not cystatins in fold.'''
+===Staphostatins resemble lipocalins, not cystatins in fold.===
-==Overview==
+<!--
-Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 A crystal structure of staphostatin B and show that the fold can be described as a fully closed, highly sheared eight-stranded beta-barrel. Thus, staphostatin B is related to beta-barrel domains that are involved in the inhibition or regulation of proteases of various catalytic types and to the superfamily of lipocalins/cytosolic fatty acid binding proteins. Unexpectedly for a cysteine protease inhibitor, staphostatin B is not significantly similar to cystatins.
+The line below this paragraph, {{ABSTRACT_PUBMED_14500882}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14500882 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14500882}}
 ==About this Structure==
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 [[Category: Sspc]]
 [[Category: Staphostatin b]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:07:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:36:48 2008''