Sandbox Reserved 779: Difference between revisions
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====Transport Protein==== | ====Transport Protein==== | ||
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== Structure of β-Lactoglobulin == | == Structure of β-Lactoglobulin == | ||
===Residues and secondary structures=== | |||
β-Lactoglobulin consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol (Cys 121). Structures of βLG have been reported by several groups with X-ray crystallography [19–21] and solution NMR [29,40,41].<ref>PMID:19362581</ref>It is a predominantly β-sheet protein. The β-barrel, or so called calyx, is conical and is made of two β-sheets: the B–D strands and N-terminal half of the A strand (denoted AN) form one sheet, and the E–H strands and C-terminal half of the A strand (denoted AC) form the other. On the outer surface of the β-barrel, between the G and H strands, is the 3-turn α-helix.The loops that connect the β-strands at the closed end of the calyx, BC, DE, and FG,are generally quite short, whereas those at the open end, AB, CD, EF,and GH, are significantly longer and more flexible. In the calyx,there is a large central cavity which is surrounded by hydrophobic residues and is accessible to solvent. This cavity provides the principal ligand-binding site. | β-Lactoglobulin consists of 162 amino acid residues (18 kDa), containing two disulfide bonds (Cys 66–Cys 160 and Cys 106–Cys 119) and a free thiol (Cys 121). Structures of βLG have been reported by several groups with X-ray crystallography [19–21] and solution NMR [29,40,41].<ref>PMID:19362581</ref>It is a predominantly β-sheet protein. The β-barrel, or so called calyx, is conical and is made of two β-sheets: the B–D strands and N-terminal half of the A strand (denoted AN) form one sheet, and the E–H strands and C-terminal half of the A strand (denoted AC) form the other. On the outer surface of the β-barrel, between the G and H strands, is the 3-turn α-helix.The loops that connect the β-strands at the closed end of the calyx, BC, DE, and FG,are generally quite short, whereas those at the open end, AB, CD, EF,and GH, are significantly longer and more flexible. In the calyx,there is a large central cavity which is surrounded by hydrophobic residues and is accessible to solvent. This cavity provides the principal ligand-binding site. | ||
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===Ligands=== | ===Ligands=== | ||
Most lipocalins bind small hydrophobic molecules within the central cup or calyx. The true function of β-Lg is unknown, but it has been suggested that it is involved in the transport of retinol and/or fatty acids [8,50]. It binds retinol with a higher affinity than does RBP [51] and, as with RBP, specific binding of retinol to β-Lg has been observed in the small intestine of the neonatal calf [3]. The structure of RBP with retinol bound within the hydrophobic calyx has been solved [2] and retinol was successfully modelled into our previous β-Lg structure [3]. β-Lg contains two tryptophans, Trp19 and Trp61, and their fluorescence is altered when retinol is bound [51].<ref>PMID:9115437</ref> | Most lipocalins bind small hydrophobic molecules within the central cup or calyx. The true function of β-Lg is unknown, but it has been suggested that it is involved in the transport of retinol and/or fatty acids [8,50]. It binds retinol with a higher affinity than does RBP [51] and, as with RBP, specific binding of retinol to β-Lg has been observed in the small intestine of the neonatal calf [3]. The structure of RBP with retinol bound within the hydrophobic calyx has been solved [2] and retinol was successfully modelled into our previous β-Lg structure [3]. β-Lg contains two tryptophans, Trp19 and Trp61, and their fluorescence is altered when retinol is bound [51].<ref>PMID:9115437</ref> | ||
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its antioxidant nature, dairy products consumed daily should not be overheated in order to maintain its antioxidant nature.<ref>PMID:17235131</ref> | its antioxidant nature, dairy products consumed daily should not be overheated in order to maintain its antioxidant nature.<ref>PMID:17235131</ref> | ||
===Bioactives transport molecule=== | |||
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===Increase Satiety, Weight Management=== | |||
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==Other β-Lactoglobulin related 3D Structures and complexes== | ==Other β-Lactoglobulin related 3D Structures and complexes== | ||
