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CRD-BP
The mouse Coding Region Determinant-Binding Protein (CRD-BP) is an RNA-binding protein.〔Doyle, G., et al. 1998. The c-myc¬ coding region determinant-binding protein: a member of a family of KH domain RNA-binding proteins. Nuc. Acid. Res. 26:5036-5044.〕 CRD-BP belongs to a family of RNA binding proteins that show close a relation to the chicken β-actin zipcode-binding protein ZBP1 〔 and the human forms of the protein IMP-1, IMP-2 and IMP-3.〔〔Liao, B., et al. 2005. The RNA-binding protein IMP-3 is a translational activator of insulin-growth factor II leader-3 mRNA during proliferation of human K562 leukemia cells. The journal of biological chemistry, 280: 18517-18524〕〔Christiansen, J., et al. 2009. IGF2 mRNA-binding protein 2: biological function and putative role in type 2 diabetes. Journal of Molecular Endocrinology, 43:187-195〕 Because of their close relationship, CRD-BP and its orthologs are thought to share the same biochemical properties. Upon binding to its transcripts, CRD-BP plays a role in translation by stabilizing and localizing the transcripts in the cell.〔 Normal expression of CRD-BP has been seen in the early development of the embryo.〔 Conversely, CRD-BP expression in adult tissue is extremely low or completely absent.〔Prokipcak, R., et al. 1994. Purification and properties of a protein that binds to the C-terminal coding region of human c-myc mRNA. Journal of Biological Chemistry, 12: 9261-9269.〕
==Structure==
CRD-BP is a 577 amino acid protein that contains 4 KH domains, 2 RRMs and a RGG box (Figure 2).〔 CRD-BP and human IMP-1 are not identical but shows a high degree of resemblance. They are very closely related to IMP-2, which has been determined through phylogenetic analysis (Figure 1).〔 As a result of this close phylogeny, the structure of the conserved functional domains is shared between CRD-BP, ZBP1 and the human IMPs (Figure 2).〔〔Chao,J., et al. 2010. ZBP1 recognition of β-actin zipcode induces RNA looping. Genes Dev, 24: 148-158.〕
The conserved KH domains are shared throughout the orthologs and they are able to form dimers which orient the RNA binding regions in a polar opposite manner (Figure 3A).〔 This orientation creates room for each G-X-X-G motif (Figure 3B) of each KH domain to bind its RNA transcript (Figure 3A).〔
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