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人源半乳糖凝集素-3 变体在缩短的 N 端尾部的两个有序片段的结晶。

Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.

机构信息

Department of Structural and Chemical Biology, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain.

Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstrabe 13, 80539, Munich, Germany.

出版信息

Sci Rep. 2018 Jun 29;8(1):9835. doi: 10.1038/s41598-018-28235-x.

DOI:10.1038/s41598-018-28235-x
PMID:29959397
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6026190/
Abstract

Among members of the family of adhesion/growth-regulatory galectins, galectin-3 (Gal-3) bears a unique modular architecture. A N-terminal tail (NT) consisting of the N-terminal segment (NTS) and nine collagen-like repeats is linked to the canonical lectin domain. In contrast to bivalent proto- and tandem-repeat-type galectins, Gal-3 is monomeric in solution, capable to self-associate in the presence of bi- to multivalent ligands, and the NTS is involved in cellular compartmentalization. Since no crystallographic information on Gal-3 beyond the lectin domain is available, we used a shortened variant with NTS and repeats VII-IX. This protein crystallized as tetramers with contacts between the lectin domains. The region from Tyr101 (in repeat IX) to Leu114 (in the CRD) formed a hairpin. The NTS extends the canonical β-sheet of F1-F5 strands with two new β-strands on the F face. Together, crystallographic and SAXS data reveal a mode of intramolecular structure building involving the highly flexible Gal-3's NT.

摘要

在黏附/生长调节半乳糖凝集素家族成员中，半乳糖凝集素-3（Gal-3）具有独特的模块化结构。由 N 端片段（NTS）和九个胶原样重复组成的 N 端尾部（NT）与经典凝集素结构域相连。与二价原和串联重复型半乳糖凝集素不同，Gal-3 在溶液中为单体，能够在双价至多价配体存在下自缔合，并且 NTS 参与细胞区室化。由于目前尚无超出凝集素结构域的 Gal-3 的晶体学信息，我们使用了带有 NTS 和重复 VII-IX 的缩短变体。该蛋白以四聚体形式结晶，在凝集素结构域之间存在接触。从 Tyr101（重复 IX）到 Leu114（在 CRD 中）的区域形成发夹结构。NTS 通过两条新的β-链扩展了 F1-F5 链的经典β-片，在 F 面上形成了两条新的β-链。晶体学和 SAXS 数据共同揭示了一种涉及高度灵活的 Gal-3 的 NT 的分子内结构构建模式。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/7559983a325c/41598_2018_28235_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/85eb7ec4f100/41598_2018_28235_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/b0d9b17847dc/41598_2018_28235_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/8e49f0bc5b3d/41598_2018_28235_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/17bcb113dd16/41598_2018_28235_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/820a8a5548fe/41598_2018_28235_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/6939b4b355ec/41598_2018_28235_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/96458eed7b0b/41598_2018_28235_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/7559983a325c/41598_2018_28235_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/85eb7ec4f100/41598_2018_28235_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/b0d9b17847dc/41598_2018_28235_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/8e49f0bc5b3d/41598_2018_28235_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/17bcb113dd16/41598_2018_28235_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/820a8a5548fe/41598_2018_28235_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/6939b4b355ec/41598_2018_28235_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/96458eed7b0b/41598_2018_28235_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ef/6026190/7559983a325c/41598_2018_28235_Fig8_HTML.jpg

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