1nyc

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[[Image:1nyc.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1nyc| PDB=1nyc | SCENE= }}
{{STRUCTURE_1nyc| PDB=1nyc | SCENE= }}
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'''Staphostatins resemble lipocalins, not cystatins in fold.'''
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===Staphostatins resemble lipocalins, not cystatins in fold.===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14500882 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14500882}}
==About this Structure==
==About this Structure==
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[[Category: Sspc]]
[[Category: Sspc]]
[[Category: Staphostatin b]]
[[Category: Staphostatin b]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:07:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:36:48 2008''

Revision as of 01:36, 28 July 2008

Image:1nyc.png

Template:STRUCTURE 1nyc

Staphostatins resemble lipocalins, not cystatins in fold.

Template:ABSTRACT PUBMED 14500882

About this Structure

1NYC is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from 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:14500882

Page seeded by OCA on Mon Jul 28 04:36:48 2008

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