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2gmc

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[[Image:2gmc.jpg|left|200px]]<br /><applet load="2gmc" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gmc" />
 
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'''Structure of C12-LF11 bound to the DPC micelles'''<br />
 
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==About this Structure==
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==Structure of C12-LF11 bound to the DPC micelles==
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2GMC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=DAO:'>DAO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GMC OCA].
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<StructureSection load='2gmc' size='340' side='right'caption='[[2gmc]]' scene=''>
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== Structural highlights ==
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==Reference==
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<table><tr><td colspan='2'>[[2gmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GMC FirstGlance]. <br>
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The acyl group as the central element of the structural organization of antimicrobial lipopeptide., Japelj B, Zorko M, Majerle A, Pristovsek P, Sanchez-Gomez S, Martinez de Tejada G, Moriyon I, Blondelle SE, Brandenburg K, Andra J, Lohner K, Jerala R, J Am Chem Soc. 2007 Feb 7;129(5):1022-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17263370 17263370]
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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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[[Category: Protein complex]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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[[Category: Japelj, B.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmc OCA], [https://pdbe.org/2gmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gmc RCSB], [https://www.ebi.ac.uk/pdbsum/2gmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gmc ProSAT]</span></td></tr>
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[[Category: DAO]]
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</table>
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[[Category: NH2]]
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== Function ==
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[[Category: helix]]
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[https://www.uniprot.org/uniprot/TRFL_HUMAN TRFL_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref>
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== References ==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:09 2008''
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Japelj B]]

Current revision

Structure of C12-LF11 bound to the DPC micelles

PDB ID 2gmc

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