Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052330 | FEBS Letters | 2006 | 7 Pages |
Abstract
The Ras-specific guanine nucleotide exchange region of hSos1 consists of two consecutive domains: the catalytic core (residues 742–1024) contains all residues binding to Ras, including the catalytic hairpin, and an upstream REM domain (residues 553–741), so called because it contains an evolutionary conserved Ras Exchange Motif (REM). We functionally define the boundaries of the REM domain through a combination of in vivo and in vitro assays. We show that an intra-REM domain interaction, mediated by phenylalanine 577, is required to allow interaction of the REM domain with the catalytic core, constraining it in the active conformation.
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Authors
Elena Sacco, David Metalli, Stefano Busti, Sonia Fantinato, Annalisa D’Urzo, Valeria Mapelli, Lilia Alberghina, Marco Vanoni,