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The lipocalins are a large family of proteins that diverse in sequence but are structurally homologous. They bind and transport small hydrophobic molecules in a central hydrophobic pocket. The lipocalin family is defined by a common fold : an eight-stranded anti-parallel β-barrel with variable loop regions flanking and enclosing the top and bottom of the barrel, to form a hydrophobic pocket.
The lipocalins are a large family of proteins that diverse in sequence but are structurally homologous. They bind and transport small hydrophobic molecules in a central hydrophobic pocket. The lipocalin family is defined by a common fold : an eight-stranded anti-parallel β-barrel with variable loop regions flanking and enclosing the top and bottom of the barrel, to form a hydrophobic pocket.
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<Structure load='2r74' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Fonction ==
== Fonction ==

Revision as of 11:09, 22 January 2017

Contents

Trichosurin : a Possum Milk Whey Lipocalin Protein

Trichosurin is one of the three predominant lipocalins found in the milk of the brushtail possum Trichosurus vulpecula. The lipocalins are a large family of proteins that diverse in sequence but are structurally homologous. They bind and transport small hydrophobic molecules in a central hydrophobic pocket. The lipocalin family is defined by a common fold : an eight-stranded anti-parallel β-barrel with variable loop regions flanking and enclosing the top and bottom of the barrel, to form a hydrophobic pocket.

Insert caption here

Drag the structure with the mouse to rotate

Fonction

In the lipocalin family, the internal topology of the hydrophobic pocket is a key factor to understand the type and the selectivity of binding. In fact, the access to the binding pocket is controlled by residues forming a loop between the β-strands at one end of the lipocalin β-barrel. Thus, the function of trichosurin is critical in metatherian lactation. But for the moment, the biochemical and biological functions of the trichosurin are not fully understood. Trichosurin may have a transporter activity for small molecules (http://www.uniprot.org/uniprot/Q29147).

Structural highlights

Forms a homodimer with four subunits.


This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

References

Proteopedia Page Contributors and Editors (what is this?)

Mina Schneider

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