1kj5: Difference between revisions

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OCA

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 ==Solution Structure of Human beta-defensin 1==
-<StructureSection load='1kj5' size='340' side='right' caption='[[1kj5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1kj5' size='340' side='right'caption='[[1kj5]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kj5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KJ5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kj5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJ5 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kj6|1kj6]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kj5 OCA], [http://pdbe.org/1kj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kj5 RCSB], [http://www.ebi.ac.uk/pdbsum/1kj5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kj5 ProSAT]</span></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=1kj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kj5 OCA], [https://pdbe.org/1kj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kj5 RCSB], [https://www.ebi.ac.uk/pdbsum/1kj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kj5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN]] Has bactericidal activity (By similarity).
+[https://www.uniprot.org/uniprot/DEFB1_HUMAN DEFB1_HUMAN] Has bactericidal activity (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kj5 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The three human beta-defensins, HBD1--3, are 33--47-residue, cationic antimicrobial proteins expressed by epithelial cells. All three proteins have broad spectrum antimicrobial activity, with HBD3 consistently being the most potent. Additionally, HBD3 has significant bactericidal activity against Gram-positive Staphylococcus aureus at physiological salt concentrations. We have compared the multimeric state of the three beta-defensins using NMR diffusion spectroscopy, dynamic and static light scattering, and analysis of the migration of the three beta-defensins on a native gel. All three techniques are in agreement, suggesting that HBD-3 is a dimer, while HBD-1 and HBD-2 are monomeric. Subsequently, the NMR solution structures of HBD1 and HBD3 were determined using standard homonuclear techniques and compared with the previously determined solution structure of HBD2. Both HBD1 and HBD3 form well defined structures with backbone root mean square deviations of 0.451 and 0.616 A, respectively. The tertiary structures of all three beta-defensins are similar, with a short helical segment preceding a three-stranded antiparallel beta-sheet. The surface charge density of each of the defensins is markedly different, with the surface of HBD3 significantly more basic. Analysis of the NMR data and structures led us to suggest that HBD3 forms a symmetrical dimer through strand beta2 of the beta-sheet. The increased anti-Staphylococcal activity of HBD3 may be explained by the capacity of the protein to form dimers in solution at low concentrations, an amphipathic dimer structure, and the increased positive surface charge compared with HBD1 and HBD2.
-The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus.,Schibli DJ, Hunter HN, Aseyev V, Starner TD, Wiencek JM, McCray PB Jr, Tack BF, Vogel HJ J Biol Chem. 2002 Mar 8;277(10):8279-89. Epub 2001 Dec 11. PMID:11741980<ref>PMID:11741980</ref>
+==See Also==
+*[[Defensin 3D structures|Defensin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1kj5" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Aseyev, V]]
+[[Category: Large Structures]]
-[[Category: Hunter, H N]]
+[[Category: Aseyev V]]
-[[Category: McCray, P B]]
+[[Category: Hunter HN]]
-[[Category: Schibli, D J]]
+[[Category: McCray Jr PB]]
-[[Category: Starner, T D]]
+[[Category: Schibli DJ]]
-[[Category: Tack, B F]]
+[[Category: Starner TD]]
-[[Category: Vogel, H J]]
+[[Category: Tack BF]]
-[[Category: Wiencek, J M]]
+[[Category: Vogel HJ]]
-[[Category: Antibiotic]]
+[[Category: Wiencek JM]]
-[[Category: Antimicrobial protein]]
-[[Category: Beta-defensin]]
-[[Category: Defensin]]
-[[Category: Hbd1]]
-[[Category: Human beta-defensin 1]]