Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin.

By H. Fehlhammer, W. Bode, R. Huber. 1977

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Protein 3D Structure Computed from Evolutionary Sequence Variation (2011, background): “Predicting the structure of proteins in the trypsin family is particularly challenging, as the structure is known to undergo a conformational change after cleavage of the activation peptide [55] and, as the N-terminal and C-terminal peptide cross from one domain to the other.”
Comparison of anionic and cationic trypsinogens: The anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure (2008, background): “Two tryptophan residues, Trp141 and Trp215, are adjacent to the activation domain~Fehlhammer et al., 1977!.”
3D Protein Structure Predicted from Sequence (2011, unknown): “10 family is particularly challenging, as the structure is known to shift somewhat after cleavage of the activation peptide[53] and, as the N-‐terminal and C-‐terminal peptide cross from one domain to the oth”