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3k0v

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{{Seed}}
 
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[[Image:3k0v.png|left|200px]]
 
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==Removal of sugars and sugars-like molecules from the solution by C-lobe of lactoferrin: Crystal structure of the complex of C-lobe with beta-D-glucopyranosyl-(1->4)-beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranose at 1.9 A resolution==
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The line below this paragraph, containing "STRUCTURE_3k0v", creates the "Structure Box" on the page.
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<StructureSection load='3k0v' size='340' side='right'caption='[[3k0v]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3k0v]] 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=3K0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K0V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
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<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=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3k0v| PDB=3k0v | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0v OCA], [https://pdbe.org/3k0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k0v RCSB], [https://www.ebi.ac.uk/pdbsum/3k0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/3k0v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3k0v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bovine lactoferrin has been shown to reduce the levels of glucose in both normal subjects and non-insulin dependent diabetic patients. The binding studies have shown that various sugar molecules interact with lactoferrin indicating the presence of a sugar-binding site in the protein. Structural studies have revealed that the sugar-binding site is located in the C-terminal half (C-lobe) of bilobal lactoferrin. Since the sugar-binding site was part of the C-lobe, it was better to carry out binding and structural studies using C-lobe rather than the full protein molecule. Therefore, C-lobe was prepared by limited proteolysis of lactoferrin with enzyme proteinase K. It was purified to homogeneity for further studies. The addition of C-lobe to human serum showed significant lowering of glucose levels. The binding studies using C-lobe with nine sugars, glucose, galactose, mannose, xylose, maltose, cellobiose, lactose, sucrose and dextrin gave values of binding constants in the range of 10(-4) to 10(-5)M. The structure determinations of the complexes of C-lobe with all the nine sugars showed that all of them interact with C-lobe through the same recognition site involving several hydrogen bonds and van der Waals interactions.
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===Removal of sugars and sugars-like molecules from the solution by C-lobe of lactoferrin: Crystal structure of the complex of C-lobe with beta-D-glucopyranosyl-(1->4)-beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranose at 1.9 A resolution===
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Specific interactions of C-terminal half (C-lobe) of lactoferrin protein with edible sugars: binding and structural studies with implications on diabetes.,Mir R, Kumar RP, Singh N, Vikram GP, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP Int J Biol Macromol. 2010 Jul 1;47(1):50-9. Epub 2010 Apr 4. PMID:20371371<ref>PMID:20371371</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3k0v" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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3K0V 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=3K0V OCA].
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*[[Lactoferrin|Lactoferrin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Kaur, P.]]
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[[Category: Large Structures]]
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[[Category: Mir, R.]]
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[[Category: Kaur P]]
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[[Category: Sharma, S.]]
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[[Category: Mir R]]
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[[Category: Singh, N.]]
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[[Category: Sharma S]]
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[[Category: Singh, T P.]]
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[[Category: Singh N]]
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[[Category: Sinha, M.]]
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[[Category: Singh TP]]
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[[Category: Vikram, G.]]
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[[Category: Sinha M]]
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[[Category: Antibiotic]]
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[[Category: Vikram G]]
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[[Category: Antimicrobial]]
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[[Category: C-lobe]]
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[[Category: Complex]]
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[[Category: Dextrin]]
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[[Category: Disulfide bond]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Iron]]
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[[Category: Iron transport]]
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[[Category: Metal-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Serine protease]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 6 05:37:40 2010''
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Current revision

Removal of sugars and sugars-like molecules from the solution by C-lobe of lactoferrin: Crystal structure of the complex of C-lobe with beta-D-glucopyranosyl-(1->4)-beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranose at 1.9 A resolution

PDB ID 3k0v

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