2gwp
From Proteopedia
(New page: 200px<br /><applet load="2gwp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gwp" /> '''High-resolution solution structure of the sa...) |
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| - | [[Image:2gwp.gif|left|200px]]<br /><applet load="2gwp" size=" | + | [[Image:2gwp.gif|left|200px]]<br /><applet load="2gwp" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4'''<br /> | '''High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha-Defensins are mediators of mammalian innate immunity, and knowledge | + | alpha-Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu(15) residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide. |
==About this Structure== | ==About this Structure== | ||
| - | 2GWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2GWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Craik, D | + | [[Category: Craik, D J.]] |
| - | [[Category: Daly, N | + | [[Category: Daly, N L.]] |
| - | [[Category: Ouellette, A | + | [[Category: Ouellette, A J.]] |
| - | [[Category: Rosengren, K | + | [[Category: Rosengren, K J.]] |
| - | [[Category: Vogel, H | + | [[Category: Vogel, H J.]] |
[[Category: beta hairpin]] | [[Category: beta hairpin]] | ||
[[Category: triple stranded beta sheet]] | [[Category: triple stranded beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:08 2008'' |
Revision as of 15:36, 21 February 2008
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High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4
Overview
alpha-Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu(15) residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.
About this Structure
2GWP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of the conserved salt bridge in mammalian paneth cell alpha-defensins: solution structures of mouse CRYPTDIN-4 and (E15D)-CRYPTDIN-4., Rosengren KJ, Daly NL, Fornander LM, Jonsson LM, Shirafuji Y, Qu X, Vogel HJ, Ouellette AJ, Craik DJ, J Biol Chem. 2006 Sep 22;281(38):28068-78. Epub 2006 Jul 20. PMID:16857681
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