Considering that the MBP-binding monobodies target the substrate-binding cleft and V H H also tends to target a functional cleft, one might expect that monobodies may only be able to bind to such a preformed cleft. The remaining Tyr residues do not contribute to this contact: Y82 lies against the backside of the Tyr cluster that forms the binding interface, and Y77 stretches away. This article has been cited by other articles in PMC. Further studies are needed to determine the general applicability of this method and the range of suitable interaction affinity. The sequences for the three loops are shown, with the numbering of Main et al. Abstract High degrees of sequence and conformation complexity found in natural protein interaction interfaces are generally considered essential for achieving tight and specific interactions.
Payton. Age: 27.
Of the seven Tyr residues in this loop Fig.
Macy. Age: 26.
High-affinity single-domain binding proteins with a binary-code interface
E Epitope mapped by NMR spectroscopy. Library construction procedures have previously been described A close-up image of the linker region with electron density is also shown. A A helical rod of the fusion proteins formed in the crystal along crystallographic 4 1 -screw axis. Amino acid sequences of individual clones identified at least two classes of monobodies for each target Fig. Interestingly, the sc value for Fab-YSd1 was likewise small, suggesting that the severe restriction of amino acid chemical diversity resulted in a poorer fit of the binding interface.