5amj | pdb_00005amj

Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with Thalidomide, Wash II structure

spinqualitylabelsall models 5amj, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5amj is a 3 chain structure with sequence from Magnetospirillum gryphiswaldense MSR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: EF2, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4TVL0_9PROT Publication Abstract from PubMed Cereblon, a primary target of thalidomide and its derivatives, has been characterized structurally from both bacteria and animals. Especially well studied is the thalidomide binding domain, CULT, which shows an invariable structure across different organisms and in complex with different ligands. Here, based on a series of crystal structures of a bacterial representative, we reveal the conformational flexibility and structural dynamics of this domain. In particular, we follow the unfolding of large fractions of the domain upon release of thalidomide in the crystalline state. Our results imply that a third of the domain, including the thalidomide binding pocket, only folds upon ligand binding. We further characterize the structural effect of the C-terminal truncation resulting from the mental-retardation linked R419X nonsense mutation in vitro and offer a mechanistic hypothesis for its irresponsiveness to thalidomide. At 1.2A resolution, our data provide a view of thalidomide binding at atomic resolution. Structural dynamics of the cereblon ligand binding domain.,Hartmann MD, Boichenko I, Coles M, Lupas AN, Hernandez Alvarez B PLoS One. 2015 May 29;10(5):e0128342. doi: 10.1371/journal.pone.0128342., eCollection 2015. PMID:26024445 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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