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F-BOX Domain
Structure:

No Image The F-box consists of three helices. The H1 helix packs orthogonally with the H2-H3 antiparallel pair. Skp2 and Skp1 interact via an interdigitated interface with the F-box sandwiched between helices of Skp1 resulting in an extensive hydrophobic contact that buries almost 3000 A2. The figure shows the structure of the F-box from human Skp2.

Structure Reference:
Schulman, BA. et al. (2000) Nature. 408(6810): 381-386. PDB: 1FS1.

Domain binding and function:
The F-box domain is a 42-48 amino acid conserved domain found at the N-terminus of F-box proteins. F-box proteins act as adaptor components of the modular E3 ubiquitin ligase SCF complex that functions in phosphorylation mediated ubiquitination. The F-box domain mediates interaction with Skp1, which links F-box proteins to a core ubiquitin-ligase complex composed of Rbx1, cdc53/Cul1 and the E2 conjugating enzyme cdc34. The C-terminal region of F-box proteins are also composed of various modular domain that interact with target substrates, often in a phosphorylation dependant manner.
Examples of Proteins: 
F-box domain protein
F-box Binding partner C-Terminal Binding partner
Cdc4 (Yeast) Skp1, Rbx1 Sic1 CDK inhibitor
Grr1 (Yeast) Skp1, Rbx1 Cyclin (CLN) 1,2
TrCp (Yeast) Skp1, Rbx1 IkB(NFkB regulator)




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