This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Clathrin
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
Clathrin is composed of <scene name='46/465441/Cv/2'>3 heavy chains (Hc) and 3 light chains (Lc) interacting in their C-termini and forming a triskelion</scene>. <ref>PMID:20493816</ref> The Hc domains are: N-terminal, ankle, distal leg, knee, proximal leg and trimerization. | Clathrin is composed of <scene name='46/465441/Cv/2'>3 heavy chains (Hc) and 3 light chains (Lc) interacting in their C-termini and forming a triskelion</scene>. <ref>PMID:20493816</ref> The Hc domains are: N-terminal, ankle, distal leg, knee, proximal leg and trimerization. | ||
| + | |||
| + | [[FirstGlance/Virus_Capsids_and_Other_Large_Assemblies#Clathrin_Coat|Clathrin Coat]] shows a small, empty clathrin coat assembly of triskelions from an electron microscopic structure, [[3iyv]]. | ||
== 3D Structures of Clathrin == | == 3D Structures of Clathrin == | ||
Revision as of 21:06, 13 November 2022
| |||||||||||
References
- ↑ Pearse BM. Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1255-9. PMID:1063406
- ↑ Wilbur JD, Hwang PK, Ybe JA, Lane M, Sellers BD, Jacobson MP, Fletterick RJ, Brodsky FM. Conformation switching of clathrin light chain regulates clathrin lattice assembly. Dev Cell. 2010 May 18;18(5):841-8. PMID:20493816 doi:10.1016/j.devcel.2010.04.007
