1h43: Difference between revisions
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<StructureSection load='1h43' size='340' side='right'caption='[[1h43]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1h43' size='340' side='right'caption='[[1h43]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h43]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1h43]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H43 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0l|1b0l]], [[1bka|1bka]], [[1cb6|1cb6]], [[1dsn|1dsn]], [[1eh3|1eh3]], [[1fck|1fck]], [[1hse|1hse]], [[1h44|1h44]], [[1h45|1h45]], [[1l5t|1l5t]], [[1lcf|1lcf]], [[1lct|1lct]], [[1lfg|1lfg]], [[1lfh|1lfh]], [[1lfi|1lfi]], [[1lgb|1lgb]], [[1vfd|1vfd]], [[1vfe|1vfe]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b0l|1b0l]], [[1bka|1bka]], [[1cb6|1cb6]], [[1dsn|1dsn]], [[1eh3|1eh3]], [[1fck|1fck]], [[1hse|1hse]], [[1h44|1h44]], [[1h45|1h45]], [[1l5t|1l5t]], [[1lcf|1lcf]], [[1lct|1lct]], [[1lfg|1lfg]], [[1lfh|1lfh]], [[1lfi|1lfi]], [[1lgb|1lgb]], [[1vfd|1vfd]], [[1vfe|1vfe]]</div></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=1h43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h43 OCA], [https://pdbe.org/1h43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h43 RCSB], [https://www.ebi.ac.uk/pdbsum/1h43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h43 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |