PMC:2724026 / 15424-16861 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":"Formation of central core formed by H1, H2, H4 and H5 (Fig. 3)\nFormation of the central core was probed by nine mutations: H1, F101A, I104A; H2, L115M, L119M; H4, V141A, L145M, W148F; and H5, H160A, L161A. The extent of helix formation was probed by 13 Ala to Gly mutations: H1, A98G, A102G; H2, A113G, A114G, A117G; H4, A138G, A139G, A142G, A143G, A146G, A150G; and H5, A166G, S167G. (Note that in native FADD DD, H1 and H5 of the central core run parallel with each other and are packed orthogonally onto the parallel helix pair H2 and H4; Fig. 1).\nIn the TS, the central core is partly formed, principally through interaction of F101 and I104 in H1, which contact residues from all the other three helices; H5 also contributes significantly to core packing, via H160 and L161 at the N-terminal end. The central core residue in H2, L115, which packs onto residues in both H1 and H5 in the native state, has a medium Φ-value. Notably, although H4 is apparently well structured, the only core residue that contributes structure in the TS is V141 at the extreme N-terminus of H4. It has a high Φ-value, and appears to pin this end of H4 to H1 via an interaction with I104. In the native state, the central core of FADD DD is dominated at one end by W148F from H4, which has a Φ-value of zero. Thus, one end of the central core appears to be largely unstructured, and H4 is essentially attached only via contacts with H2 (via the B2 core).","divisions":[{"label":"title","span":{"begin":0,"end":62}},{"label":"p","span":{"begin":63,"end":550}}],"tracks":[]}