2gwp: Difference between revisions

Revision as of 09:48, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2gwp.png

Template:STRUCTURE 2gwp

High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4

Template:ABSTRACT PUBMED 16857681

About this StructureAbout this Structure

2GWP is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''High-resolution solution structure of the salt-bridge defficient mouse defensin (E15D)-Cryptdin4'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16857681}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16857681 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16857681}}
 ==About this Structure==
-GWP is a [[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].
+GWP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWP OCA].
 ==Reference==
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 [[Category: Beta hairpin]]
 [[Category: Triple stranded beta sheet]]
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