2h4i
From Proteopedia
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| == Structural highlights == | == Structural highlights == | ||
| <table><tr><td colspan='2'>[[2h4i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H4I FirstGlance]. <br> | <table><tr><td colspan='2'>[[2h4i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H4I FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=LBT:ALPHA-LACTOSE'>LBT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=LBT:ALPHA-LACTOSE'>LBT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | 
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nkx|1nkx]], [[2b65|2b65]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nkx|1nkx]], [[2b65|2b65]]</td></tr> | 
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h4i RCSB], [http://www.ebi.ac.uk/pdbsum/2h4i 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=2h4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h4i RCSB], [http://www.ebi.ac.uk/pdbsum/2h4i PDBsum]</span></td></tr> | 
| - | <table> | + | </table> | 
| + | == Function == | ||
| + | [[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]] | ||
| + | == References == | ||
| + | <references/> | ||
| __TOC__ | __TOC__ | ||
| </StructureSection> | </StructureSection> | ||
| [[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Kaur, P | + | [[Category: Kaur, P]] | 
| - | [[Category: Mir, R | + | [[Category: Mir, R]] | 
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] | 
| - | [[Category: Singh, N | + | [[Category: Singh, N]] | 
| - | [[Category: Singh, T P | + | [[Category: Singh, T P]] | 
| - | [[Category: Sinha, M | + | [[Category: Sinha, M]] | 
| - | [[Category: Kumar, R Prem | + | [[Category: Kumar, R Prem]] | 
| [[Category: C-lobe]] | [[Category: C-lobe]] | ||
| [[Category: Complex]] | [[Category: Complex]] | ||
Revision as of 10:43, 25 December 2014
Crystal structure of the complex of proteolytically produced C-terminal half of bovine lactoferrin with lactose at 2.55 A resolution
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Categories: Bos taurus | Kaur, P | Mir, R | Sharma, S | Singh, N | Singh, T P | Sinha, M | Kumar, R Prem | C-lobe | Complex | Lactoferrin | Lactose | Metal binding protein

