CaltechAUTHORS
  A Caltech Library Service

Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL

Kozak, John J. and Gray, Harry B. and Garza-López, Roberto A. and Wangkanont, Kittikhun (2018) Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL. Journal of Inorganic Biochemistry, 185 . pp. 86-102. ISSN 0162-0134. http://resolver.caltech.edu/CaltechAUTHORS:20180502-085201827

[img] PDF - Accepted Version
See Usage Policy.

1789Kb
[img] PDF (Supplementary data) - Supplemental Material
See Usage Policy.

224Kb

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20180502-085201827

Abstract

We extend our study of the structural stability of helical and nonhelical regions in chain A of human intelectin-1 to include a second human intelectin (4WMY) and the frog protein “Xenopus embryonic epidermal lectin” (XEEL). These unique lectins have been shown to recognize carbohydrate residues found exclusively in microbes, thus they could potentially be developed into novel microbe detection and sequestration tools. We believe that by studying the structural stability of these proteins we can provide insights on their biological role and activities. Using a geometrical model introduced previously, we perform computational analyses of protein crystal structures that quantify the resiliency of the native state to steric perturbations. Based on these analyses, we conclude that differences in the resiliency of the human and frog proteins can be attributed primarily to differences in non-helical regions and to residues near Ca ions. Since these differences are particularly pronounced in the vicinity of the ligand binding site, they provide an explanation for the finding that human intelectin-1 has a higher affinity for a ligand than XEEL. We also present data on conserved and position-equivalent pairs of residues in 4WMY and XEEL. We identify residue pairs as well as regions in which the influence of neighboring residues is nearly uniform as the parent protein denatures. Since the structural signatures are conserved, this identification provides a basis for understanding why both proteins exhibit trimeric structures despite poor sequence conservation at the interface.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1016/j.jinorgbio.2018.04.021DOIArticle
Additional Information:© 2018 Elsevier Inc. Received 23 December 2017, Revised 10 April 2018, Accepted 30 April 2018, Available online 2 May 2018. We thank NIH (R01 DK019038 to HBG) for support of work performed at the California Institute of Technology. Financial support for R.A.G.-L. was provided in part by grant # 52007555 to Pomona College from the Howard Hughes Medical Institute through the Precollege and Undergraduate Science Education Program. KW was supported in part by Grants for Development of New Faculty Staff, Ratchadaphiseksomphot Endowment Fund (Grant no. GDNS 59-059-23-020 and DNS 61-011-23-003-2), Chulalongkorn University and the Research Fund for DPST Graduate with First Placement [Grant no. 018/2559] from the Institute for the Promotion of Teaching Science and Technology (IPST), Thailand. Molecular graphics images were produced using the Chimera package from the Computer Graphics Laboratory, University of California, San Francisco (supported by NIH P41RR-01081).
Funders:
Funding AgencyGrant Number
NIHR01 DK019038
Howard Hughes Medical Institute (HHMI)52007555
Ratchadaphiseksomphot Endowment FundGDNS 59-059-23-020
Ratchadaphiseksomphot Endowment FundDNS 61-011-23-003-2
Chulalongkorn UniversityUNSPECIFIED
Institute for the Promotion of Teaching Science and Technology (IPST)018/2559
NIHP41RR-01081
Record Number:CaltechAUTHORS:20180502-085201827
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20180502-085201827
Official Citation:John J. Kozak, Harry B. Gray, Roberto A. Garza-López, Kittikhun Wangkanont, Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL, Journal of Inorganic Biochemistry, Volume 185, 2018, Pages 86-102, ISSN 0162-0134, https://doi.org/10.1016/j.jinorgbio.2018.04.021. (http://www.sciencedirect.com/science/article/pii/S0162013417309091)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:86186
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:03 May 2018 21:23
Last Modified:04 Jun 2018 21:01

Repository Staff Only: item control page