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Article

Virtual screening on an α-helix to β-strand switchable region of the FGFR2 extracellular domain revealed positive and negative modulators.

Proteins - 1 Nov 2014

Diaz Constantino, Corentin Herbert, Thierry Vermat, Chantal Alcouffe, Tanguy Bozec, David Sibrac, Jean-Marc Herbert, Pascual Ferrara, Françoise Bono, Edgardo Ferran

Abstract excerpt

The secondary structure of some protein segments may vary between α-helix and β-strand. To predict these switchable segments, we have developed an algorithm, Switch-P, based solely on the protein sequence. This algorithm was used on the extracellular parts of FGF receptors. For FGFR2, it predicted that β4 and β5 strands of the third Ig-like domain were highly switchable. These two strands possess a high number of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Mitogen-Activated Protein Kinase 1

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Share to Receptor, Fibroblast Growth Factor, Type 2

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Source

Identifiers

PMID: 25082719
DOI: 10.1002/prot.24657

Genes

FGFR2
FGF7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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