Sandbox Reserved 779: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 15: Line 15:


β-Lactoglobulin (β-LG)is the major whey protein of ruminant species. Its amino-acid sequence and 3-dimensional structure show that it is a lipocalin, a widely diverse family, most of which bind small hydrophobic ligands and thus may act as specific transporters, as does serum retinol binding protein <ref>PMID:15259212</ref>.
β-Lactoglobulin (β-LG)is the major whey protein of ruminant species. Its amino-acid sequence and 3-dimensional structure show that it is a lipocalin, a widely diverse family, most of which bind small hydrophobic ligands and thus may act as specific transporters, as does serum retinol binding protein <ref>PMID:15259212</ref>.
Dimeric Lactoglobulin molecules exist in the open conformation at basic pH, whereas they exist in the closed conformation at acidic pH, after undergoing Tanford transition around neutral pH. <ref>PMID:17932936</ref>
<ref>PMID:16368109</ref>
<ref>PMID:9760236</ref>


Bovine b-lactoglobulin (b-Lg) is a much studied and commercially important whey protein with an as yet undetermined function,
Bovine b-lactoglobulin (b-Lg) is a much studied and commercially important whey protein with an as yet undetermined function,
although it is of obvious nutritional value. b-Lg binds a variety of ligands and by comparison of the general structures of these
although it is of obvious nutritional value. b-Lg binds a variety of ligands and by comparison of the general structures of these
molecules together with several competition studies, it appears that there are at least 3 independent binding sites.  
molecules together with several competition studies, it appears that there are at least 3 independent binding sites.  
In the absence of
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.
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>


Line 31: Line 32:


[[Image:Beta_lac_2Q2M.png|thumb|right|320px|Bovine Beta-Lactoglobulin Native_2Q2M]]
[[Image:Beta_lac_2Q2M.png|thumb|right|320px|Bovine Beta-Lactoglobulin Native_2Q2M]]
===Relevant background ===
===Relevant background ===
class of protein :Belongs to the calycin superfamily. Lipocalin family.
class of protein :Belongs to the calycin superfamily. Lipocalin family.
overall function of Lipocalin family: The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids.
overall function of Lipocalin family: The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids.
Retrieved from "https://proteopedia.org/Sandbox_Reserved_779"