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1bka

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{{Seed}}
 
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[[Image:1bka.png|left|200px]]
 
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==OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN==
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The line below this paragraph, containing "STRUCTURE_1bka", creates the "Structure Box" on the page.
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<StructureSection load='1bka' size='340' side='right'caption='[[1bka]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bka]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BKA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene></td></tr>
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{{STRUCTURE_1bka| PDB=1bka | SCENE= }}
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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=1bka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bka OCA], [https://pdbe.org/1bka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bka RCSB], [https://www.ebi.ac.uk/pdbsum/1bka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bka ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/1bka_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1bka ConSurf].
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<div style="clear:both"></div>
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===OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN===
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==See Also==
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*[[Lactoferrin|Lactoferrin]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_8703903}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 8703903 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_8703903}}
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==About this Structure==
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1BKA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKA OCA].
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==Reference==
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Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin., Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN, Biochemistry. 1996 Jul 16;35(28):9007-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8703903 8703903]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baker, E N.]]
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[[Category: Baker EN]]
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[[Category: Baker, H M.]]
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[[Category: Baker HM]]
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[[Category: Smith, C A.]]
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[[Category: Smith CA]]
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[[Category: Anion binding]]
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[[Category: Iron binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:17:53 2008''
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Current revision

OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN

PDB ID 1bka

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