Structural Stability of Intelectin-1.

We study the structural stability of helical and nonhelical regions in chain A of human intelectin-1. Using a geometrical model introduced previously, we carried out a computational analysis based on the recently reported crystal structure of this protein by Kiessling et al. to quantify the resiliency of the native state to steric perturbations. Response to these perturbations is characterized by calculating, relative to the native state, the lateral, radial, and angular displacements of n-residue segments of the polypeptide chain centered on each residue. By quantifying the stability of the protein through six stages of unfolding, we are able to identify regions in chain A of intelectin-1 that are markedly affected by structural perturbations versus those that are relatively unaffected, the latter suggesting that the native-state geometry of these regions is essentially conserved. Importantly, residues in the vicinity of calcium ions comprise a conserved region, suggesting that Ca ions play a role not only in the coordination of carbohydrate hydroxyl groups but also in preserving the integrity of the structure.