PubMed:11251120 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"protein"},{"id":"T2","span":{"begin":36,"end":53},"obj":"protein"},{"id":"T3","span":{"begin":91,"end":96},"obj":"protein"},{"id":"T4","span":{"begin":141,"end":160},"obj":"protein"},{"id":"T5","span":{"begin":345,"end":358},"obj":"protein"},{"id":"T6","span":{"begin":360,"end":364},"obj":"protein"},{"id":"T7","span":{"begin":387,"end":392},"obj":"protein"},{"id":"T8","span":{"begin":486,"end":490},"obj":"protein"},{"id":"T9","span":{"begin":501,"end":506},"obj":"protein"},{"id":"T10","span":{"begin":595,"end":609},"obj":"protein"},{"id":"T11","span":{"begin":620,"end":625},"obj":"protein"},{"id":"T12","span":{"begin":648,"end":652},"obj":"protein"},{"id":"T13","span":{"begin":711,"end":715},"obj":"protein"},{"id":"T14","span":{"begin":766,"end":774},"obj":"protein"},{"id":"T15","span":{"begin":823,"end":828},"obj":"protein"},{"id":"T16","span":{"begin":878,"end":882},"obj":"protein"},{"id":"T17","span":{"begin":883,"end":888},"obj":"protein"},{"id":"T18","span":{"begin":933,"end":938},"obj":"protein"},{"id":"T19","span":{"begin":1009,"end":1014},"obj":"protein"},{"id":"T20","span":{"begin":1015,"end":1023},"obj":"protein"}],"text":"Structure of an extracellular gp130 cytokine receptor signaling complex.\nThe activation of gp130, a shared signal-transducing receptor for a family of cytokines, is initiated by recognition of ligand followed by oligomerization into a higher order signaling complex. Kaposi's sarcoma-associated herpesvirus encodes a functional homolog of human interleukin-6 (IL-6) that activates human gp130. In the 2.4 angstrom crystal structure of the extracellular signaling assembly between viral IL-6 and human gp130, two complexes are cross-linked into a tetramer through direct interactions between the immunoglobulin domain of gp130 and site III of viral IL-6, which is necessary for receptor activation. Unlike human IL-6 (which uses many hydrophilic residues), the viral cytokine largely uses hydrophobic amino acids to contact gp130, which enhances the complementarity of the viral IL-6-gp130 binding interfaces. The cross-reactivity of gp130 is apparently due to a chemical plasticity evident in the amphipathic gp130 cytokine-binding sites."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":30,"end":35},"obj":"protein"},{"id":"T2","span":{"begin":91,"end":96},"obj":"protein"},{"id":"T3","span":{"begin":345,"end":358},"obj":"protein"},{"id":"T4","span":{"begin":360,"end":364},"obj":"protein"},{"id":"T5","span":{"begin":387,"end":392},"obj":"protein"},{"id":"T6","span":{"begin":486,"end":490},"obj":"protein"},{"id":"T7","span":{"begin":501,"end":506},"obj":"protein"},{"id":"T8","span":{"begin":620,"end":625},"obj":"protein"},{"id":"T9","span":{"begin":648,"end":652},"obj":"protein"},{"id":"T10","span":{"begin":711,"end":715},"obj":"protein"},{"id":"T11","span":{"begin":823,"end":828},"obj":"protein"},{"id":"T12","span":{"begin":878,"end":882},"obj":"protein"},{"id":"T13","span":{"begin":883,"end":888},"obj":"protein"},{"id":"T14","span":{"begin":933,"end":938},"obj":"protein"},{"id":"T15","span":{"begin":1009,"end":1014},"obj":"protein"}],"text":"Structure of an extracellular gp130 cytokine receptor signaling complex.\nThe activation of gp130, a shared signal-transducing receptor for a family of cytokines, is initiated by recognition of ligand followed by oligomerization into a higher order signaling complex. Kaposi's sarcoma-associated herpesvirus encodes a functional homolog of human interleukin-6 (IL-6) that activates human gp130. In the 2.4 angstrom crystal structure of the extracellular signaling assembly between viral IL-6 and human gp130, two complexes are cross-linked into a tetramer through direct interactions between the immunoglobulin domain of gp130 and site III of viral IL-6, which is necessary for receptor activation. Unlike human IL-6 (which uses many hydrophilic residues), the viral cytokine largely uses hydrophobic amino acids to contact gp130, which enhances the complementarity of the viral IL-6-gp130 binding interfaces. The cross-reactivity of gp130 is apparently due to a chemical plasticity evident in the amphipathic gp130 cytokine-binding sites."}