3QIL
Crystal structure analysis of the clathrin trimerization domain
Summary for 3QIL
| Entry DOI | 10.2210/pdb3qil/pdb |
| Descriptor | Clathrin heavy chain 1 (1 entity in total) |
| Functional Keywords | clathrin trimerization domain, endocytosis, structural protein |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P49951 |
| Total number of polymer chains | 24 |
| Total formula weight | 354210.65 |
| Authors | Ybe, J.A.,Mishra, S.,Nix, J. (deposition date: 2011-01-27, release date: 2012-02-01, Last modification date: 2024-02-21) |
| Primary citation | Ybe, J.A.,Fontaine, S.N.,Stone, T.,Nix, J.,Lin, X.,Mishra, S. Nuclear localization of clathrin involves a labile helix outside the trimerization domain. Febs Lett., 587:142-149, 2013 Cited by PubMed Abstract: Clathrin is a trimeric protein involved in receptor-mediated-endocytosis, but can function as a non-trimer outside of endocytosis. We have discovered that the subcellular distribution of a clathrin cysteine mutant we previously studied is altered and a proportion is also localized to nuclear spaces. MALS shows C1573A hub is a mixture of trimer-like and detrimerized molecules. The X-ray structure of the trimerization domain reveals that without light chains, a helix harboring cysteine-1573 is reoriented. We propose clathrin has a detrimerization switch, which suggests clathrin topology can be altered naturally for new functions. PubMed: 23178717DOI: 10.1016/j.febslet.2012.11.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.92 Å) |
Structure validation
Download full validation report
