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Published November 23, 2016 | Accepted Version
Journal Article Open

Structural Stability of Intelectin-1

Abstract

We study the structural stability of helical and non-helical regions in chain A of human intelectin-1. Using a geometrical model introduced previously, a computational analysis based on the recently reported crystal structure of this protein by Kiessling et al. [Nature Struct. Mole. Bio. 22 (2015), 603] is carried out 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 which are markedly affected by structural perturbations versus those which 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 in preserving the integrity of the structure.

Additional Information

© 2016 American Chemical Society. Received 28 August 2016. Publication Date (Web): October 26, 2016. We are delighted that our work is included in the special issue of Journal of Physical Chemistry in honor of Professor Mark Gordon, an all-around good guy who has made groundbreaking contributions to the quantum chemistry of atoms and molecules. His development of (the computational program) GAMESS has had a big impact on the field. One of the authors (JJK) is indebted to Dr. K. Wangkanont for clarifying details of the crystal structure of the lectin proteins cited in the Discussion. We thank the National Institutes of Health (R01 DK 019038 to HBG) for support of work performed at the California Institute of Technology. Financial support for R.A.G.-L. was provided by the Howard Hughes Medical Institute Research Program from Pomona College. The molecular graphics images were produced using the Chimera package from the Computer Graphics Laboratory, University of California, San Francisco (supported by NIH P41 RR-01081).

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