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2dwi
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2dwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dwi, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:2dwi.jpg|left|200px]]<br /><applet load="2dwi" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2dwi, resolution 2.20Å" /> | ||
| - | '''Crystal structure of the complex formed between C-terminal half of bovine lactoferrin and cellobiose at 2.2 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of the complex formed between C-terminal half of bovine lactoferrin and cellobiose at 2.2 A resolution== |
| - | + | <StructureSection load='2dwi' size='340' side='right'caption='[[2dwi]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [[ | + | <table><tr><td colspan='2'>[[2dwi]] is a 1 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=2DWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DWI FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <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>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2dwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dwi OCA], [https://pdbe.org/2dwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dwi RCSB], [https://www.ebi.ac.uk/pdbsum/2dwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dwi ProSAT]</span></td></tr> |
| - | [ | + | </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> |
| - | + | == Evolutionary Conservation == | |
| - | [ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | [ | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/2dwi_consurf.spt"</scriptWhenChecked> |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | [[ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [ | + | </jmolCheckbox> |
| - | [[ | + | </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=2dwi ConSurf]. |
| - | + | <div style="clear:both"></div> | |
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Lactoferrin|Lactoferrin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bhushan A]] | ||
| + | [[Category: Kaur P]] | ||
| + | [[Category: Mir R]] | ||
| + | [[Category: Prem Kumar R]] | ||
| + | [[Category: Sharma S]] | ||
| + | [[Category: Singh N]] | ||
| + | [[Category: Singh TP]] | ||
| + | [[Category: Sinha M]] | ||
Current revision
Crystal structure of the complex formed between C-terminal half of bovine lactoferrin and cellobiose at 2.2 A resolution
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Categories: Bos taurus | Large Structures | Bhushan A | Kaur P | Mir R | Prem Kumar R | Sharma S | Singh N | Singh TP | Sinha M
