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3o97

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o97 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o97 RCSB], [http://www.ebi.ac.uk/pdbsum/3o97 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o97 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o97 RCSB], [http://www.ebi.ac.uk/pdbsum/3o97 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Lactoferrin|Lactoferrin]]
*[[Lactoferrin|Lactoferrin]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 20:19, 24 December 2014

Crystal Structure of the complex of C-lobe of lactoferrin with indole acetic acid at 2.68 A Resolution

3o97, resolution 2.68Å

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