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. Author manuscript; available in PMC: 2015 Oct 1.
Published in final edited form as: Glycoconj J. 2014 Oct;31(0):417–426. doi: 10.1007/s10719-014-9556-4

Figure 3. Schematic of the part of TSR that interacts with Pofut2.

Figure 3

A) Truncated TSR4 from F-spondin used in experiments to demonstrate essential structural elements required for substrate recognition by Pofut2 [59].

B) Distribution of various residues of a TSR involved in enzyme-substrate reaction. Of about 30 sites involved in enzyme interaction, 10 are conserved (amongst known Pofut2 substrates), 9 are solvent exposed, and the rest have highly variable side-chains. While specific residues in the active site interact with the conserved regions of the TSR, large cavities in the substrate-binding pocket can accommodate the variable side chains [59].