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Related Experiment Video

Updated: Dec 28, 2025

Expression, Purification, and Antimicrobial Activity of S100A12

Expression, Purification, and Antimicrobial Activity of S100A12

Published on: May 13, 2017

S100A7/Ran-binding protein 9 coevolution in mammals.

Fabio D'Amico¹, Francesca Nadalin², Massimo Libra³

¹Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy. f.damico@unict.it.

|February 12, 2020

Summary

This summary is machine-generated.

Coevolutionary analysis reveals a significant link between S100A7 and Ran-binding protein 9 (RanBP9), suggesting amino acid variations impact their interaction and potentially disease pathogenesis.

Keywords:

Coevolution Mammals RanBP9 S100A7

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Last Updated: Dec 28, 2025

Expression, Purification, and Antimicrobial Activity of S100A12

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Published on: May 13, 2017

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Published on: September 29, 2019

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Published on: September 3, 2014

Area of Science:

Molecular Biology
Evolutionary Biology
Immunology

Background:

S100A7 and Ran-binding protein 9 (RanBP9) are key immune response effectors.
Functional protein interactions are driven by coevolution.
Vertebrate coevolution mechanisms between S100A7 and RanBP9 are not well understood.

Purpose of the Study:

To investigate the coevolutionary mechanisms between S100A7 and RanBP9 in vertebrates.
To identify potential pathogenic effects arising from variations in S100A7/RanBP9 interactions.

Main Methods:

Protein coevolution analysis using Mirrortree to calculate correlation coefficients between inter-protein distance matrices.
Utilized the Blocks in Sequences (BIS2) algorithm via the BIS2Analyzer webserver for coevolutionary analysis, leveraging RanBP9's high vertebrate conservation.

Main Results:

A moderate overall correlation (R=0.53, p<1e-06) was found between S100A7 and RanBP9 inter-protein distances.
A significant coevolution cluster was identified between S100A7 and RanBP9 (p<8.10e-05).

Conclusions:

Coevolutionary analysis supports a functional interaction between S100A7 and RanBP9.
Amino acid variations may modulate the S100A7/RanBP9 interaction, potentially leading to pathogenic effects.
Findings may guide future research on S100A7 and RanBP9 functions and drug development for related diseases.