2kht: Difference between revisions
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<StructureSection load='2kht' size='340' side='right'caption='[[2kht]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2kht' size='340' side='right'caption='[[2kht]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kht]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2kht]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHT FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEF1, DEFA1, DEFA2, MRS ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEF1, DEFA1, DEFA2, MRS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kht OCA], [https://pdbe.org/2kht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kht RCSB], [https://www.ebi.ac.uk/pdbsum/2kht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kht ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:05, 1 December 2021
NMR Structure of human alpha defensin HNP-1NMR Structure of human alpha defensin HNP-1
Structural highlights
Publication Abstract from PubMedHuman alpha-defensins [human neutrophil peptides (HNPs)] are immune defense mini-proteins that act by disrupting microbial cell membranes. Elucidating the three-dimensional (3D) structures of HNPs in lipid membranes is important for understanding their mechanisms of action. Using solid-state NMR (SSNMR), we have determined the 3D structure of HNP-1 in a microcrystalline state outside the lipid membrane, which provides benchmarks for structure determination and comparison with the membrane-bound state. From a suite of two-dimensional and 3D magic-angle spinning experiments, (13)C and (15)N chemical shifts that yielded torsion angle constraints were obtained, while inter-residue distances were obtained to restrain the 3D fold. Together, these constraints led to the first high-resolution SSNMR structure of a human defensin. The SSNMR structure has close similarity to the crystal structures of the HNP family, with the exception of the loop region between the first and second beta-strands. The difference, which is partially validated by direct torsion angle measurements of selected loop residues, suggests possible conformational variation and flexibility of this segment of the protein, which may regulate HNP interaction with the phospholipid membrane of microbial cells. Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.,Zhang Y, Doherty T, Li J, Lu W, Barinka C, Lubkowski J, Hong M J Mol Biol. 2010 Mar 26;397(2):408-22. Epub 2010 Jan 22. PMID:20097206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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