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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. | 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 understood. | + | 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 == | == Structural highlights == | ||
| + | Forms a homodimer with four subunits. | ||
Revision as of 10:01, 22 January 2017
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.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
