PMC:2724026 / 35591-37347 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2724026","sourcedb":"PMC","sourceid":"2724026","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2724026","text":"The structure of FADD DD compared to Ig-like and spectrin domains. (a) FADD DD (PDB code 1E41) is composed of two three-helix bundles packed orthogonally. Bundle 1 (red) comprises helices 1, 5 and 6; bundle 2 (blue) comprises helices 2, 3 and 4. (b) An alternative view of FADD DD showing that the central region of the protein has two pairs of parallel helices packing against each other (green), H1 and H5 from bundle 1 and H2 and H4 from bundle 2. H3 and H6 are peripheral to the structure and make contacts only within their respective bundles. (c) FADD DD has three structurally distinct cores: two formed by each three-helix bundle (red and blue) and a central core formed by packing of the two pairs of central helices (green). (d) A diagram showing the 2-D topology of FADD DD. Five of the helices display classical Greek key topology.19,20 The helices are coloured to distinguish between bundle 1 (red) and bundle 2 (blue). The helix that is not part of the Greek key motif is shown in pale red. (e) Greek key Ig-like domains (in this case, TNfn3, PDB code 1ten) comprise two anti-parallel pairs of strands (one pair from each sheet, shown in green) which pack against each other to form the centre of the single hydrophobic core. Ig-like domains differ in the number and arrangement of peripheral strands (shown in red and blue to distinguish the sheets). (f) A diagram showing the 2-D topology of TNfn3. Five of the strands display classical Greek key topology. The two sheets are coloured in red and blue. Strands that are not part of the Greek key motif are shown in pale colours. (g) Spectrin domains (in this case spectrin R16 from PDB code 1cun) are simple three-helix bundles with the same up-down-up arrangement as the bundles of FADD DD.","tracks":[]}