Evidence map›Paper›PMID 40929095›Full record

ArticleBioinformatics (Oxford, England)2025

ProteinLIPs: a web server for identifying highly polar and poorly packed interfaces in proteins.

Helena García-Cebollada, Alfonso López, Vladimir E Angarica, Juan José Galano-Frutos, Javier Sancho

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Article in Bioinformatics (Oxford, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Helena García-CebolladaBiocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, 50018 Zaragoza, Spain.
Alfonso LópezBiocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, 50018 Zaragoza, Spain.
Vladimir E AngaricaBiocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, 50018 Zaragoza, Spain.
Juan José Galano-FrutosBiocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0002-1896-7805
Javier SanchoBiocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit GBsC-CSIC, University of Zaragoza, 50018 Zaragoza, Spain.ORCID 0000-0002-2879-9200

Funding

European Union's Horizon 2020, MOSBRI EFA080/01
6 · The paper itself

Abstract

motivationThe stability of protein interfaces influences protein dynamics and unfolding cooperativity. Although in some cases the dynamics of proteins can be deduced from their topology, much of the stability of an interface is related to the complementarity of the interacting parts. It is also important to note that proteins that display non-cooperative unfolding cannot be rationally stabilized unless the regions that unfold first are known. Being able to identify protein interfaces that are significantly less stable would contribute to our understanding of protein dynamics and be very valuable in guiding the rational stabilization of proteins with non-two-state unfolding equilibria.

resultsWe introduce ProteinLIPs, a web server that detects interfaces of high polarity and low packing density, termed LIPs. Each LIP consist of a continuous sequence segment (mLIP) plus its contacting residues (cLIP). ProteinLIPs scans monomeric and oligomeric proteins and provides graphical sequence profiles and interactive 3D visualizations of the detected LIPs. Statistical analysis of 53 protein domains from 10 superfamilies shows the two parts of a LIP present distinct characteristics. mLIPs are conserved, structurally unstable and enriched in polar residues, whereas cLIPs are more stable, less conserved, and enriched in apolar residues. Besides, cLIPs are enriched in small-molecule binding site residues, suggesting they play a role in ligand interaction, likely facilitated by instability of the associated mLIPs. ProteinLIPs provides a user-friendly platform for the automated identification and visualization of LIPs and can be used to guide the engineering of non-two-state proteins where LIPs constitute preferential targets for thermostabilization. AVAILABILITY AND IMPLEMENTATION: ProteinLIPs is publicly available at https://lips.bifi.es/.

Indexed as

ProteinsSoftwareDatabases, ProteinInternetModels, MolecularProtein ConformationProteins

Identifiers

PMID40929095
PMCPMC12457736

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.