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4ib7

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Revision as of 11:12, 5 August 2016

Bovine beta-lactoglobulin (isoform A) in complex with dodecyltrimethylammonium (DTAC)

Structural highlights

4ib7 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3ueu, 4ib6, 4ib8, 4ib9, 4iba
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.

Publication Abstract from PubMed

Isoforms A (LGB-A) and B (LGB-B) of bovine lactoglobulin, the milk protein, differ in positions 64 (D<-->G) and 118 (V<-->A). Interactions of LGB-A and LGB-B with sodium dodecyl sulfate (SDS), dodecyltrimethylammonium chloride (DTAC) and lauric acid (LA), 12-carbon ligands possessing differently charged polar groups, were investigated using isothermal titration calorimetry and X-ray crystallography, to study the proton linkage phenomenon and to distinguish between effects related to different isoforms and different ligand properties. The determined values of DeltaS and DeltaH revealed that for all ligands, binding is entropically driven. The contribution from enthalpy change is lower and shows strong dependence on type of buffer that indicates proton release from the protein varying with protein isoform and ligand type and involvement of LA and Asp64 (in isoform A) in this process. The ligand affinities for both isoforms were arranged in the same order, DTAC < LA < SDS, and were systematically lower for variant B. The entropy change of the complexation process was always higher for isoform A, but these values were compensated by changes in enthalpy, resulting in almost identical DeltaG for complexes of both isoforms. The determined crystal structures showed that substitution in positions 64 and 118 did not influence the overall structure of LGB complexes. The chemical character of the ligand polar group did not affect the position of its aliphatic chain in protein beta-barrel, indicating a major role of hydrophobic interactions in ligand binding that prevailed even with the repulsion between positively charged DTAC and lysine residues located at binding site entrance. Copyright (c) 2013 John Wiley & Sons, Ltd.

The differences in binding 12-carbon aliphatic ligands by bovine beta-lactoglobulin isoform A and B studied by isothermal titration calorimetry and X-ray crystallography.,Loch JI, Bonarek P, Polit A, Swiatek S, Dziedzicka-Wasylewska M, Lewinski K J Mol Recognit. 2013 Aug;26(8):357-67. doi: 10.1002/jmr.2280. PMID:23784992^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Loch JI, Bonarek P, Polit A, Swiatek S, Dziedzicka-Wasylewska M, Lewinski K. The differences in binding 12-carbon aliphatic ligands by bovine beta-lactoglobulin isoform A and B studied by isothermal titration calorimetry and X-ray crystallography. J Mol Recognit. 2013 Aug;26(8):357-67. doi: 10.1002/jmr.2280. PMID:23784992 doi:10.1002/jmr.2280

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ib7"

@@ Line 1: / Line 1: @@
 ==Bovine beta-lactoglobulin (isoform A) in complex with dodecyltrimethylammonium (DTAC)==
 <StructureSection load='4ib7' size='340' side='right' caption='[[4ib7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAT:DODECANE-TRIMETHYLAMINE'>CAT</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ueu|3ueu]], [[4ib6|4ib6]], [[4ib8|4ib8]], [[4ib9|4ib9]], [[4iba|4iba]]</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=4ib7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ib7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ib7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ib7 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=4ib7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ib7 OCA], [http://pdbe.org/4ib7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ib7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ib7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ib7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ib7" style="background-color:#fffaf0;"></div>
 ==See Also==

4ib7

From Proteopedia

Revision as of 11:12, 5 August 2016

Bovine beta-lactoglobulin (isoform A) in complex with dodecyltrimethylammonium (DTAC)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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