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==Crystal structure of pepsin cleaved C-terminal half of lactoferrin at 2.7A resolution== | ==Crystal structure of pepsin cleaved C-terminal half of lactoferrin at 2.7A resolution== | ||
<StructureSection load='7ev0' size='340' side='right'caption='[[7ev0]]' scene=''> | <StructureSection load='7ev0' size='340' side='right'caption='[[7ev0]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EV0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ev0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EV0 FirstGlance]. <br> | ||
</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=7ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ev0 OCA], [https://pdbe.org/7ev0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ev0 RCSB], [https://www.ebi.ac.uk/pdbsum/7ev0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ev0 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7ev0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ev0 OCA], [https://pdbe.org/7ev0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ev0 RCSB], [https://www.ebi.ac.uk/pdbsum/7ev0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ev0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN] 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:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</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:8980754</ref> <ref>PMID:15222473</ref> | |||
==See Also== | |||
*[[Lactoferrin|Lactoferrin]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ahmad MI]] | [[Category: Ahmad MI]] | ||
Latest revision as of 20:04, 29 November 2023
Crystal structure of pepsin cleaved C-terminal half of lactoferrin at 2.7A resolutionCrystal structure of pepsin cleaved C-terminal half of lactoferrin at 2.7A resolution
Structural highlights
FunctionTRFL_BOVIN Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.[1] [2] Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.[3] [4] Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.[5] [6] 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.[7] [8] See AlsoReferences
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