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- Publisher
- Wiley
- Copyright
- Copyright © 1995 The Protein Society
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- DOI
- 10.1002/pro.5560040920
- pmid
- 8528083
- Publisher site
- See Article on Publisher Site
Abstract
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 was 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.
Journal
Protein Science – Wiley
Published: Sep 1, 1995