2kd2 | pdb_00002kd2

NMR Structure of FAIM-CTD

spinqualitylabelsall models 2kd2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kd2 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FAIM1_MOUSE Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Fas apoptosis inhibitory molecule (FAIM) is a soluble cytosolic protein inhibitor of programmed cell death and is found in organisms throughout the animal kingdom. A short isoform of FAIM is expressed in all tissue types, while an alternatively spliced long isoform is specifically expressed in the brain. Here, the short isoform is shown to consist of two independently folding domains in contact with each other. The NMR solution structure of the C-terminal domain of murine FAIM is solved in isolation and revealed to be a novel protein fold, a noninterleaved seven-stranded beta-sandwich. The structure and sequence reveal several residues that are likely to be involved in functionally significant interactions with the N-terminal domain or other binding partners. Chemical shift perturbation is used to elucidate contacts made between the N-terminal domain and the C-terminal domain. Fas Apoptosis Inhibitory Molecule Contains a Novel beta-Sandwich in Contact with a Partially Ordered Domain.,Hemond M, Rothstein TL, Wagner G J Mol Biol. 2009 Jan 13. PMID:19168072 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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