Evidence from sequence information that the interleukin-1 receptor is a transmembrane GTPase
| العنوان: | Evidence from sequence information that the interleukin-1 receptor is a transmembrane GTPase |
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| المؤلفون: | Thomas P. Hopp |
| المصدر: | Protein Science. 4:1851-1859 |
| بيانات النشر: | Wiley, 1995. |
| سنة النشر: | 1995 |
| مصطلحات موضوعية: | Chemical Phenomena, GTP', Protein Conformation, Molecular Sequence Data, Sequence Homology, GTPase, Interleukin-1 receptor, Biology, Biochemistry, Protein Structure, Secondary, Homology (biology), GTP Phosphohydrolases, Phosphates, Magnesium, Amino Acid Sequence, Molecular Biology, Conserved Sequence, chemistry.chemical_classification, Binding Sites, Chemistry, Physical, Effector, Cell Membrane, Receptors, Interleukin-1, Hydrogen Bonding, Peptide Fragments, Transmembrane protein, Amino acid, chemistry, Cytoplasm, Guanosine Triphosphate, Signal Transduction, Research Article |
| الوصف: | Evidence is presented that the cytoplasmic domain of the type I interleukin-1 receptor (IL-1R) may be a GTPase. This domain conserves segments of hydrophobic amino acids that suggest a structural relatedness to the ras protooncogene protein and other members of the GTPase superfamily, despite a lack of significant detectable sequence homology. When the hydrophobic segments of the IL-1R were aligned with similar segments of the GTPases, it became apparent that the IL-1Rs possess a number of conserved amino acids that represent plausible functional residues for base-specific binding of GTP, magnesium chelation, and phosphate ester hydrolysis. Furthermore, a segment of five contiguous residues were found that is identical between ras and the IL-1R, and which is positioned to form part of the guanine base binding pocket. If this model is correct, then the IL-1Rs possess a highly conserved effector protein binding region, but one that is entirely unrelated to the effector regions of other superfamily members. Therefore, if the IL-1R is indeed a GTPase, then its activation function may be directed to as-yet unrecognized effector target proteins, as part of a unique cellular signal transduction pathway. |
| تدمد: | 1469-896X 0961-8368 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::842dcc378bac685ba2d5a5e2629297e5 https://doi.org/10.1002/pro.5560040920 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....842dcc378bac685ba2d5a5e2629297e5 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1469896X 09618368 |
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