1nyc: Difference between revisions

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


{{Structure
<!--
|PDB= 1nyc |SIZE=350|CAPTION= <scene name='initialview01'>1nyc</scene>, resolution 1.40&Aring;
The line below this paragraph, containing "STRUCTURE_1nyc", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= staphostatin B (sspC) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
-->
|DOMAIN=
{{STRUCTURE_1nyc| PDB=1nyc  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyc OCA], [http://www.ebi.ac.uk/pdbsum/1nyc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nyc RCSB]</span>
}}


'''Staphostatins resemble lipocalins, not cystatins in fold.'''
'''Staphostatins resemble lipocalins, not cystatins in fold.'''
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[[Category: Rzychon, M.]]
[[Category: Rzychon, M.]]
[[Category: Sabat, A.]]
[[Category: Sabat, A.]]
[[Category: cysteine protease inhibitor]]
[[Category: Cysteine protease inhibitor]]
[[Category: sspc]]
[[Category: Sspc]]
[[Category: staphostatin b]]
[[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 Sun Mar 30 22:37:13 2008''

Revision as of 03:07, 3 May 2008

File:1nyc.jpg

Template:STRUCTURE 1nyc

Staphostatins resemble lipocalins, not cystatins in fold.


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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:14500882 Page seeded by OCA on Sat May 3 03:07:54 2008

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