2gto
From Proteopedia
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| - | [[Image:2gto.jpg|left|200px]] | + | [[Image:2gto.jpg|left|200px]] |
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| - | '''Oxidized form of ADAP hSH3-N''' | + | {{Structure |
| + | |PDB= 2gto |SIZE=350|CAPTION= <scene name='initialview01'>2gto</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FYB, SLAP130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Oxidized form of ADAP hSH3-N''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GTO is a [ | + | 2GTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTO OCA]. |
==Reference== | ==Reference== | ||
| - | Redox-regulated conformational changes in an SH3 domain., Zimmermann J, Kuhne R, Sylvester M, Freund C, Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. PMID:[http:// | + | Redox-regulated conformational changes in an SH3 domain., Zimmermann J, Kuhne R, Sylvester M, Freund C, Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17511475 17511475] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helically extended sh3 domain (hsh3)]] | [[Category: helically extended sh3 domain (hsh3)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:08:57 2008'' |
Revision as of 15:09, 20 March 2008
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| Gene: | FYB, SLAP130 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Oxidized form of ADAP hSH3-N
Overview
Oxidation-induced conformational changes in proteins provide a powerful mechanism to sense the redox state of a living cell. In contrast to the unspecific and often irreversible oxidation of intracellular proteins during severe oxidative stress, regulatory redox events need to have specific and transient effects on cellular targets. Here we present evidence for the reversible formation of a vicinal disulfide bond in a prototypic protein interaction domain. NMR spectroscopy was used to determine the structure of the N-terminal hSH3 domain (hSH3N) of the immune cell protein ADAP (adhesion and degranulation promoting adapter protein) in the reduced and oxidized states. An eight-membered ring formed upon oxidation of two neighboring cysteines leads to significant changes in the variable arginine-threonine (RT) loop of the hSH3N domain and alters the helix-sheet packing of the domain. The redox potential for this structural transition is -228 mV at pH 7.4. This is compatible with a role of the cysteinylcysteine moiety in redox signaling during T cell activation.
About this Structure
2GTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Redox-regulated conformational changes in an SH3 domain., Zimmermann J, Kuhne R, Sylvester M, Freund C, Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. PMID:17511475
Page seeded by OCA on Thu Mar 20 17:08:57 2008
