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7ev0
From Proteopedia
(Difference between revisions)
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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]] | ||
Current revision
Crystal structure of pepsin cleaved C-terminal half of lactoferrin at 2.7A resolution
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Categories: Bos taurus | Large Structures | Ahmad MI | Maurya A | Sharma P | Sharma S | Singh J | Singh TP
