2lew: Difference between revisions

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-[[Image:2lew.png|left|200px]]
-<!--
+==Structural Plasticity of Paneth cell alpha-Defensins: Characterization of Salt-Bridge Deficient Analogues of Mouse Cryptdin-4==
-The line below this paragraph, containing "STRUCTURE_2lew", creates the "Structure Box" on the page.
+<StructureSection load='2lew' size='340' side='right'caption='[[2lew]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2lew]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LEW FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lew OCA], [https://pdbe.org/2lew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lew RCSB], [https://www.ebi.ac.uk/pdbsum/2lew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lew ProSAT]</span></td></tr>
-{{STRUCTURE_2lew|  PDB=2lew  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DEFA4_MOUSE DEFA4_MOUSE] Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Salt-bridge interactions between acidic and basic amino acids contribute to the structural stability of proteins and to protein-protein interactions. A conserved salt-bridge is a canonical feature of the alpha-defensin antimicrobial peptide family, but the role of this common structural element has not been fully elucidated. We have investigated mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and peptide variants with mutations at Arg(7) or Glu(15) residue positions to disrupt the salt-bridge and assess the consequences on Crp4 structure, function, and stability. NMR analyses showed that both (R7G)-Crp4 and (E15G)-Crp4 adopt native-like structures, evidence of fold plasticity that allows peptides to reshuffle side chains and stabilize the structure in the absence of the salt-bridge. In contrast, introduction of a large hydrophobic side chain at position 15, as in (E15L)-Crp4 cannot be accommodated in the context of the Crp4 primary structure. Regardless of which side of the salt-bridge was mutated, salt-bridge variants retained bactericidal peptide activity with differential microbicidal effects against certain bacterial cell targets, confirming that the salt-bridge does not determine bactericidal activity per se. The increased structural flexibility induced by salt-bridge disruption enhanced peptide sensitivity to proteolysis. Although sensitivity to proteolysis by MMP7 was unaffected by most Arg(7) and Glu(15) substitutions, every salt-bridge variant was degraded extensively by trypsin. Moreover, the salt-bridge facilitates adoption of the characteristic alpha-defensin fold as shown by the impaired in vitro refolding of (E15D)-proCrp4, the most conservative salt-bridge disrupting replacement. In Crp4, therefore, the canonical alpha-defensin salt-bridge facilitates adoption of the characteristic alpha-defensin fold, which decreases structural flexibility and confers resistance to degradation by proteinases.
-===Structural Plasticity of Paneth cell alpha-Defensins: Characterization of Salt-Bridge Deficient Analogues of Mouse Cryptdin-4===
+The alpha-defensin salt-bridge induces backbone stability to facilitate folding and confer proteolytic resistance.,Andersson HS, Figueredo SM, Haugaard-Kedstrom LM, Bengtsson E, Daly NL, Qu X, Craik DJ, Ouellette AJ, Rosengren KJ Amino Acids. 2012 Jan 29. PMID:22286872<ref>PMID:22286872</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2lew" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_22286872}}, adds the Publication Abstract to the page
+*[[Defensin 3D structures|Defensin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 22286872 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_22286872}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[2lew]] is a 1 chain structure with 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=2LEW OCA].
-==Reference==
-<ref group="xtra">PMID:022286872</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Andersson, H S.]]
+[[Category: Andersson HS]]
-[[Category: Bengtsson, E.]]
+[[Category: Bengtsson E]]
-[[Category: Craik, D J.]]
+[[Category: Craik DJ]]
-[[Category: Daly, N L.]]
+[[Category: Daly NL]]
-[[Category: Haugaard-Kedstrom, L M.]]
+[[Category: Haugaard-Kedstrom LM]]
-[[Category: Rosengren, K.]]
+[[Category: Rosengren K]]
-[[Category: Antimicrobial protein]]