1l4v

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Current revision (06:56, 30 October 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1l4v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sarcophaga_peregrina Sarcophaga peregrina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4V FirstGlance]. <br>
<table><tr><td colspan='2'>[[1l4v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sarcophaga_peregrina Sarcophaga peregrina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 18 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=1l4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4v OCA], [https://pdbe.org/1l4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4v RCSB], [https://www.ebi.ac.uk/pdbsum/1l4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4v 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=1l4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4v OCA], [https://pdbe.org/1l4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4v RCSB], [https://www.ebi.ac.uk/pdbsum/1l4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4v ProSAT]</span></td></tr>
</table>
</table>
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/1l4v_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/1l4v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</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=1l4v ConSurf].
</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=1l4v ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.
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1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.,Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y FEBS Lett. 1990 Sep 3;269(2):413-20. PMID:2401368<ref>PMID:2401368</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1l4v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

SOLUTION STRUCTURE OF SAPECIN

PDB ID 1l4v

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