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Clathrin (CLT) is a component of vesicle coast.[1]
Structural highlights
Clathrin is composed of 3 heavy chains (Hc) and 3 light chains (Lc) interacting in their C-termini and forming a triskelion. 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
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3D Structures of Clathrin
Updated on 15-December-2015
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- clathrin
- 1bpo – 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, 2xzh, 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
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