3qil | pdb_00003qil

Crystal structure analysis of the clathrin trimerization domain

spinqualitylabelsall models 3qil, resolution 3.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qil is a 24 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CLTC (Bos taurus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Nuclear localization of clathrin involves a labile helix outside the trimerization domain.,Ybe JA, Fontaine SN, Stone T, Nix J, Lin X, Mishra S FEBS Lett. 2013 Jan 16;587(2):142-9. doi: 10.1016/j.febslet.2012.11.005. Epub, 2012 Nov 21. PMID:23178717 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clathrin

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