5ZC0

Crystal structure of Xenopus embryonic epidermal lectin in complex with Samarium ions

5ZC0 の概要

• エントリーDOI: 10.2210/pdb5zc0/pdb
• 分子名称: Xenopus Embryonic Epidermal Lectin, CALCIUM ION, SAMARIUM (III) ION, ... (4 entities in total)
• 機能のキーワード: carbohydrate binding protein, lectin, intelectin, xeel, samarium, sugar binding protein
• 由来する生物種: Xenopus laevis (African clawed frog)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 194458.83

構造登録者

Wangkanont, K. (登録日: 2018-02-14, 公開日: 2018-06-06, 最終更新日: 2024-11-06)

主引用文献

Kozak, J.J.,Gray, H.B.,Garza-Lopez, R.A.,Wangkanont, K.
Structural stabilities of calcium proteins: Human intelectin-1 and frog lectin XEEL
J. Inorg. Biochem., 185:86-102, 2018

PubMed 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.

PubMed: 29807191
DOI: 10.1016/j.jinorgbio.2018.04.021

実験手法

X-RAY DIFFRACTION (2.75 Å)