Sandbox Reserved 779: Difference between revisions
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<Structure load='2Q2M' size='400' frame='true' align='right' caption='Native β-Lactoglobulin(β-LG)' scene='Insert optional scene name here' /> | <Structure load='2Q2M' size='400' frame='true' align='right' caption='Native β-Lactoglobulin(β-LG)' scene='Insert optional scene name here' /> | ||
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In the absence of direct crystallographic evidence, a preliminary modelling study reveals that there is an internal cavity which can readily accommodate retinol in a manner similar to the related lipocalin, retinol-binding protein. On the outer surface, a solvent-accessible hydrophobic cleft runs between the 3-turn a-helix that is packed against the outer surface of the b-barrel. This cleft can accommodate fatty acids like palmitate and stearate. | In the absence of direct crystallographic evidence, a preliminary modelling study reveals that there is an internal cavity which can readily accommodate retinol in a manner similar to the related lipocalin, retinol-binding protein. On the outer surface, a solvent-accessible hydrophobic cleft runs between the 3-turn a-helix that is packed against the outer surface of the b-barrel. This cleft can accommodate fatty acids like palmitate and stearate. | ||
<ref>http://www.sciencedirect.com/science/article/pii/S0958694698000211</ref> | <ref>http://www.sciencedirect.com/science/article/pii/S0958694698000211</ref> | ||
β-Lactoglobulin is a small protein, soluble in dilute salt solution as befits a globulin, with 162 amino acid residues (Mr ∼18,400) that fold up into an 8-stranded, antiparallel β-barrel with a 3-turn α-helix on the outer surface and a ninth β-strand flanking the first strand (see Figure 1). It is this strand that forms a significant part of the dimer interface in the bovine and bovine proteins but, while still present in porcine β-LG, is not involved in the formation of the dimer that forms at low pH. | β-Lactoglobulin is a small protein, soluble in dilute salt solution as befits a globulin, with 162 amino acid residues (Mr ∼18,400) that fold up into an 8-stranded, antiparallel β-barrel with a 3-turn α-helix on the outer surface and a ninth β-strand flanking the first strand (see Figure 1). It is this strand that forms a significant part of the dimer interface in the bovine and bovine proteins but, while still present in porcine β-LG, is not involved in the formation of the dimer that forms at low pH. | ||
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They also maintain the organization of apical surfaces on the plasma membrane <ref>PMID:11329377</ref>. | They also maintain the organization of apical surfaces on the plasma membrane <ref>PMID:11329377</ref>. | ||
== Structure of β-LG == | |||
==Structure | == Overview of Crystalline Structure == | ||
βLG consists of 162 amino acid residues (18 kDa), containing two | βLG consists of 162 amino acid residues (18 kDa), containing two | ||
