View source for 1nyc

[[Image:1nyc.jpg|left|200px]]<br /><applet load="1nyc" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1nyc, resolution 1.40&Aring;" />
'''Staphostatins resemble lipocalins, not cystatins in fold.'''<br />

==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.

==About this Structure==
1NYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with CL and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NYC OCA]. 

==Reference==
Staphostatins resemble lipocalins, not cystatins in fold., Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M, Protein Sci. 2003 Oct;12(10):2252-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14500882 14500882]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Bochtler, M.]]
[[Category: Dubin, A.]]
[[Category: Filipek, R.]]
[[Category: Kosowska, K.]]
[[Category: Potempa, J.]]
[[Category: Rzychon, M.]]
[[Category: Sabat, A.]]
[[Category: CL]]
[[Category: SO4]]
[[Category: cysteine protease inhibitor]]
[[Category: sspc]]
[[Category: staphostatin b]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:39:31 2007''