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[[Image: | ==Crystal Structure of the Complex of C-lobe of Bovine Lactoferrin with Dextrin at 1.9 A Resolution== | ||
<StructureSection load='3kj7' size='340' side='right' caption='[[3kj7]], [[Resolution|resolution]] 1.91Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3kj7]] 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=3KJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KJ7 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=CTR:CELLOTRIOSE'>CTR</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dwa|2dwa]], [[2dxy|2dxy]], [[3ibo|3ibo]]</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=3kj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kj7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kj7 RCSB], [http://www.ebi.ac.uk/pdbsum/3kj7 PDBsum]</span></td></tr> | |||
<table> | |||
== 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/kj/3kj7_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Lactoferrin|Lactoferrin]] | *[[Lactoferrin|Lactoferrin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Kaur, P.]] | [[Category: Kaur, P.]] | ||
Revision as of 15:37, 29 September 2014
Crystal Structure of the Complex of C-lobe of Bovine Lactoferrin with Dextrin at 1.9 A ResolutionCrystal Structure of the Complex of C-lobe of Bovine Lactoferrin with Dextrin at 1.9 A Resolution
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBovine 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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