Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Nov 20;14:7551. doi: 10.1038/s41467-023-43148-8

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 5 — a Structural superimposition of the mGFRα1^D2-D3-SOS complex (PDB: 2V5E) with an intact zGFRα1^D1-D3 (PDB: 7AML) shown as a ribbon representation (left) and a surface rendering coloured according to Columbic electrostatic potential (right). mGFRα1^D2-D3 cartoon coloured grey with D2 light grey and D3 in dark grey. zGFRα1^D1-D3 cartoon coloured in green with D1 light green, D2 green and D3 dark green. SOS ligand, shown as sticks, binds to a positively charged cleft formed between all three domains. b Steric clash between D1 domain of zGFRα1^D1-D3 (PDB: 7AML) and zGFRα1^D2-D3 pentamers within the decameric complex. zGFRα1^D2-D3 pentamer shown as a surface representation coloured according to electrostatic surface potential. mGFRα1^D2-D3-SOS complex (PDB: 2V5E) is superposed onto zGFRα1^D1-D3 shown as cartoon coloured in green with D1 light green, D2 green and D3 dark green. Superimpositions were done in UCSF ChimeraX using the MatchMaker tool⁸⁵. c ITC analysis of hGFRα1 interactions with HS. (i) hGFRα1^D1-CT binding to HS dp10 and (ii) hGFRα1^D2-CT binding to HS dp10. Raw ITC titration data plotted against time (top) and integrated heat signals plotted as a function of molar ratio (bottom). Circles represent the integrated heat of interaction, while blue curves represent the best fit obtained by non-linear least-squares procedures using the “One set of sites” model. Representative titrations and binding curves are shown. Derived binding constants (Kds) are reported on each plot, as mean values of ≥3 independent experiments ± standard deviation. d, e D1 domain impact of GAGs binding to mGFRα1 in the HEK293 adhesion assay. HEK293T cells were transfected with vector alone, mGFRα1^FL or mGFRα1^ΔD1 with GFP. GFP-expressing cells were preincubated with SOS (d) or HS (e) for 2 h in the absence of GDNF. GDNF was then added for an additional 2 h at room temperature. The percentage of cells in aggregates greater than 5 cells under the indicated conditions is shown. Mean values of triplicate experiments ± s.e.m. (d) *p = 0.0306, **p = 0.0059, ***p = 0.0004, ****p < 0.0001, ^#p = 0.0268, (e) **p = 0.021, ***p = 0.0003, ^#p = 0.0013, ^##p = 0.004. One-way ANOVA, followed by Tukey´s multiple comparison test.