Sandbox Reserved 707: Difference between revisions
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As we distinguished before, there are 3 types of RAF proteins: A-RAF, B-RAF and C-RAF. All of them share 3 much conserved regions (CR): CR1, CR2 and <scene name='Sandbox_Reserved_707/Cr3_domain/2'>CR3</scene>. We have to say here that in the pdb file 1UWH the protein is already dimerized (as we will say it in the next part), and so we have here '''two''' CR3 domains. <br /> | As we distinguished before, there are 3 types of RAF proteins: A-RAF, B-RAF and C-RAF. All of them share 3 much conserved regions (CR): CR1, CR2 and <scene name='Sandbox_Reserved_707/Cr3_domain/2'>CR3</scene><ref>PMID:15520807</ref>. We have to say here that in the pdb file 1UWH the protein is already dimerized (as we will say it in the next part), and so we have here '''two''' CR3 domains. <br /> | ||
CR1 is composed of a RAS binding domain (RBD) and a cysteine rich domain (CRD) which can bind 2 zinc ions (zinc finger domain). It is possible for the CR1 to interact with the RAS and with the membrane phospholipids (PH domain). <br /> | CR1 is composed of a RAS binding domain (RBD) and a cysteine rich domain (CRD) which can bind 2 zinc ions (zinc finger domain). It is possible for the CR1 to interact with the RAS and with the membrane phospholipids (PH domain). <br /> | ||
CR2 is a serine threonine rich domain. When a serine is phosphorylated this domain can bind a regulatory protein that can bind the C-terminal region in the same time. Binding of 14-3-3 (C-terminal region) to this phosphorylated serine is inhibitory for the enzyme.<br /> | CR2 is a serine threonine rich domain. When a serine is phosphorylated this domain can bind a regulatory protein that can bind the C-terminal region in the same time. Binding of 14-3-3 (C-terminal region) to this phosphorylated serine is inhibitory for the enzyme.<br /> | ||
