Sandbox8999: Difference between revisions
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[[Clathrin]] | [[Clathrin]] | ||
{{STRUCTURE_3lvg| PDB=3lvg | SIZE=400| SCENE= |right|CAPTION=Bovine clathrin heavy (grey, green, pink) and light (yellow, magenta, cyan) chains, [[3lvg]] }} | {{STRUCTURE_3lvg| PDB=3lvg | SIZE=400| SCENE= |right|CAPTION=Bovine clathrin heavy (grey, green, pink) and light (yellow, magenta, cyan) chains, [[3lvg]] }} | ||
The word clathrin originates from the Latin word clāthrāre, meaning “to provide with a lattice”. Clathrin is a protein involved in receptor-mediated endocytosis. <ref name="harrison"> Harrison, S. C., Kirchhausen, T., & Owen, D. (2014). Molecular structure, function, and dynamics of clathrin-mediated membrane traffic. ''Cold Spring Harbor Perspectives in Biology.'' [http://dx.doi.org/10.1101/cshperspect.a016725 doi: 10.1101/cshperspect.a016725]</ref> It was not discovered until 1975 by Barbara Pearse, a British biological scientist. Clathrin is a protein resembling a triskelion shape and is composed of three heavy chains and three light chains which come together to form a polyhedral lattice similar to a cage.<ref name="harrison" /> The three heavy chains resemble three legs protruding from a center point. Some of the major functions of clathrin include lysosomal targeting, receptor-mediated endocytosis, and organelle biogenesis from the trans-Golgi network. <ref name="wakeham">Wakeham, D. E., et al. (2003). Clathrin self-assembly involves coordinated weak interactions favorable for cellular recognition. ''The Embo Journal.'' [http://dx.doi.org/10.1093/emboj/cdg511 doi: 10.1093/emboj/cdg511]</ref>. The polyhedral lattice shape of clathrin largely determines its functionality, in that there are many binding sites for proteins on the heavy chains of the lattice as well. <ref name="ungewickell">Ungewickell, E., & Brandon, D. (1981). Assembly units of clathrin coats. ''Nature, 289'', 420-42. [http://dx.doi.org/10.1038/289420a0 doi: 10.1038/289420a0]</ref> | |||
== Structure == | == Structure == | ||