Clathrin

Clathrin heavy N-terminal propeller repeat
Clathrin terminal domain
Identifiers
Symbol	Clathrin_propel
Pfam	PF01394
Pfam clan	CL0020
InterPro	IPR022365
SCOP2	1bpo / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Clathrin heavy-chain linker
clathrin heavy chain proximal repeat (linker)
Identifiers
Symbol	Clathrin-link
Pfam	PF09268
Pfam clan	CL0020
InterPro	IPR015348
SCOP2	1b89 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated by Barbara Pearse in 1976.^[1] It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle. The protein's name refers to this lattice structure, deriving from Latin clathri meaning lattice.^[2] Barbara Pearse named the protein clathrin at the suggestion of Graeme Mitchison, selecting it from three possible options.^[3] Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation. The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection.^[4]