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| | <StructureSection load='1uz2' size='340' side='right'caption='[[1uz2]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='1uz2' size='340' side='right'caption='[[1uz2]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uz2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UZ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uz2]] 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=1UZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UZ2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0o|1b0o]], [[1b8e|1b8e]], [[1beb|1beb]], [[1bso|1bso]], [[1bsq|1bsq]], [[1bsy|1bsy]], [[1cj5|1cj5]], [[1dv9|1dv9]], [[1gx8|1gx8]], [[1gx9|1gx9]], [[1gxa|1gxa]], [[1mfh|1mfh]], [[1qg5|1qg5]], [[2blg|2blg]], [[3blg|3blg]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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=1uz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uz2 OCA], [http://pdbe.org/1uz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uz2 RCSB], [http://www.ebi.ac.uk/pdbsum/1uz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uz2 ProSAT]</span></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=1uz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uz2 OCA], [https://pdbe.org/1uz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1uz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uz2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | + | [https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Haertle, T]] | + | [[Category: Haertle T]] |
| - | [[Category: Holt, C]] | + | [[Category: Holt C]] |
| - | [[Category: Jayat, D]] | + | [[Category: Jayat D]] |
| - | [[Category: McNae, I]] | + | [[Category: McNae I]] |
| - | [[Category: Sawyer, L]] | + | [[Category: Sawyer L]] |
| - | [[Category: Allergen]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Milk]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Whey retinol-binding]]
| + | |
| Structural highlights
Function
LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
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 PubMed
The lipocalin beta-lactoglobulin (BLG) is the major whey protein of bovine milk and is homodimeric at physiological conditions. Each monomer contains two disulfide bonds and one cysteine at position 121 (C121). This free thiol plays an important role in the heat-induced aggregation of BLG and, possibly, in its conformational stability. We describe here the expression in the yeast Pichia pastoris of a mutant bovine BLG, in which C121 was changed into Ser (C121S). Circular dichroism and high-performance liquid chromatography experiments, together with the X-ray crystal structure, show that the C121S mutant retains a nativelike fold at both neutral and acid pH. The mutation completely blocks the irreversible aggregation induced by heat treatment at 90 degrees C. Compared to the recombinant wild-type protein, the mutant is less stable to temperature and disulfide reducing agents and is much more sensitive to peptic digestion. Moreover, its affinity for 1-anilino-8-naphthalenesulfonate is increased at neutral and acid pH. We suggest that the stability of the protein arising from the hydrophobic effect is reduced by the C121S mutation so that unfolded or partially unfolded states are more favored.
A recombinant C121S mutant of bovine beta-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating.,Jayat D, Gaudin JC, Chobert JM, Burova TV, Holt C, McNae I, Sawyer L, Haertle T Biochemistry. 2004 May 25;43(20):6312-21. PMID:15147215[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jayat D, Gaudin JC, Chobert JM, Burova TV, Holt C, McNae I, Sawyer L, Haertle T. A recombinant C121S mutant of bovine beta-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating. Biochemistry. 2004 May 25;43(20):6312-21. PMID:15147215 doi:10.1021/bi0362469
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