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| **[[1c9i]], [[1c9l]] - rCLT Hc N terminal + B-adaptin 3<br /> | | **[[1c9i]], [[1c9l]] - rCLT Hc N terminal + B-adaptin 3<br /> |
| **[[2xzg]], [[2xzh]], [[4g55]]- CLT Hc N terminal + pitstop inhibitor - human<br /> | | **[[2xzg]], [[4g55]]- CLT Hc N terminal + pitstop inhibitor - human<br /> |
| **[[1utc]] - bCLT Hc N terminal + amphiphysin peptide<br /> | | **[[1utc]] - bCLT Hc N terminal + amphiphysin peptide<br /> |
| **[[1xi5]] - bCLT Hc + auxilin J-domain – Cryo EM<br /> | | **[[1xi5]] - bCLT Hc + auxilin J-domain – Cryo EM<br /> |
Revision as of 11:16, 14 November 2016
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Clathrin (CLT) is a component of vesicle coast.[1] For details see Clathrin JMU.
Structural highlights
Clathrin is composed of 3 heavy chains (Hc) and 3 light chains (Lc) interacting in their C-termini and forming a triskelion. [2] The Hc domains are: N-terminal, ankle, distal leg, knee, proximal leg and trimerization.
- ↑ 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
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3D Structures of Clathrin
Updated on 14-November-2016
{"openlevels":0}
- clathrin
- Clathrin JMU – rCLT Hc N terminal domain + linker – rat
- 1b89 – bCLT Hc proximal leg – bovine
- 3qil - bCLT Hc trimerization domain
- 3lvg - bCLT Hc + Lc
- 3lvh - bCLT Hc HUB fragment + Lc
- 1xi4, 3iyv – bCLT Hc + Lc – Cryo EM
- Clathrin binary complexes
- 1c9i, 1c9l - rCLT Hc N terminal + B-adaptin 3
- 2xzg, 4g55- CLT Hc N terminal + pitstop inhibitor - human
- 1utc - bCLT Hc N terminal + amphiphysin peptide
- 1xi5 - bCLT Hc + auxilin J-domain – Cryo EM
- 3gc3 – bCLT Hc WD domain + b-arrestin-1
- 3gd1 - bCLT Hc + Hc WD domain + b-arrest
References
