4fh0 | pdb_00004fh0

Crystal Structure of Human BinCARD CARD, double mutant F16M/L66M SeMet form

spinqualitylabelsall models 4fh0, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fh0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAR19_HUMAN Plays a role in inhibiting the effects of BCL10-induced activation of NF-kappa-B. May inhibit the phosphorylation of BCL10 in a CARD-dependent manner. Publication Abstract from PubMed The caspase recruitment domain (CARD) is present in death-domain superfamily proteins involved in inflammation and apoptosis. BinCARD is named for its ability to interact with Bcl10 and inhibit downstream signalling. Human BinCARD is expressed as two isoforms that encode the same N-terminal CARD region but which differ considerably in their C-termini. Both isoforms are expressed in immune cells, although BinCARD-2 is much more highly expressed. Crystals of the CARD fold common to both had low symmetry (space group P1). Molecular replacement was unsuccessful in this low-symmetry space group and, as the construct contains no methionines, first one and then two residues were engineered to methionine for MAD phasing. The double-methionine variant was produced as a selenomethionine derivative, which was crystallized and the structure was solved using data measured at two wavelengths. The crystal structures of the native and selenomethionine double mutant were refined to high resolution (1.58 and 1.40 A resolution, respectively), revealing the presence of a cis-peptide bond between Tyr39 and Pro40. Unexpectedly, the native crystal structure revealed that all three cysteines were oxidized. The mitochondrial localization of BinCARD-2 and the susceptibility of its CARD region to redox modification points to the intriguing possibility of a redox-regulatory role. The structure of the caspase recruitment domain of BinCARD reveals that all three cysteines can be oxidized.,Chen KE, Richards AA, Caradoc-Davies TT, Vajjhala PR, Robin G, Lua LH, Hill JM, Schroder K, Sweet MJ, Kellie S, Kobe B, Martin J Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):774-84. doi:, 10.1107/S0907444913001558. Epub 2013 Apr 11. PMID:23633586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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