Version 1
: Received: 1 April 2024 / Approved: 2 April 2024 / Online: 2 April 2024 (08:52:56 CEST)
How to cite:
Visibelli, A.; Finetti, R.; Niccolai, N.; Spiga, O.; Santucci, A. Molecular Origins of the Mendelian Rare Diseases Reviewed by Orpha.net: A Structural Bioinformatics Investigation. Preprints2024, 2024040156. https://doi.org/10.20944/preprints202404.0156.v1
Visibelli, A.; Finetti, R.; Niccolai, N.; Spiga, O.; Santucci, A. Molecular Origins of the Mendelian Rare Diseases Reviewed by Orpha.net: A Structural Bioinformatics Investigation. Preprints 2024, 2024040156. https://doi.org/10.20944/preprints202404.0156.v1
Visibelli, A.; Finetti, R.; Niccolai, N.; Spiga, O.; Santucci, A. Molecular Origins of the Mendelian Rare Diseases Reviewed by Orpha.net: A Structural Bioinformatics Investigation. Preprints2024, 2024040156. https://doi.org/10.20944/preprints202404.0156.v1
APA Style
Visibelli, A., Finetti, R., Niccolai, N., Spiga, O., & Santucci, A. (2024). Molecular Origins of the Mendelian Rare Diseases Reviewed by Orpha.net: A Structural Bioinformatics Investigation. Preprints. https://doi.org/10.20944/preprints202404.0156.v1
Chicago/Turabian Style
Visibelli, A., Ottavia Spiga and Annalisa Santucci. 2024 "Molecular Origins of the Mendelian Rare Diseases Reviewed by Orpha.net: A Structural Bioinformatics Investigation" Preprints. https://doi.org/10.20944/preprints202404.0156.v1
Abstract
The study of rare diseases is important not only for the individuals affected but also for the advancement of medical knowledge and a deeper understanding of human biology and genetics. The wide repertoire of structural information now available from reliable and accurate prediction methods provides the opportunity to investigate the molecular origins of most of the rare diseases reviewed in the Orpha.net database. Thus, it has been possible to analyze the topology of the missense mutations found in the 2,535 proteins involved in Mendelian rare diseases (MRD), which form the database for our structural bioinformatics study. The amino acid substitutions responsible for MRD show different mutation site distributions at different three-dimensional protein depths. We then predicted the depth-dependent effects of mutations for the 20,248 pathogenic variants that are present in our database. The results of this structural bioinformatics investigation are relevant, as they provide additional clues to mitigate the damage caused by MRD.
Keywords
rare diseases; missense mutations; protein structure; databank analysis; structural bioinformatics
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
