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Article

Role of the EHD2 unstructured loop in dimerization, protein binding and subcellular localization.

PloS one - 1 Jan 2015

Bahl Kriti, Naslavsky Naava, Caplan Steve

Abstract excerpt

The C-terminal Eps 15 Homology Domain proteins (EHD1-4) play important roles in regulating endocytic trafficking. EHD2 is the only family member whose crystal structure has been solved, and it contains an unstructured loop consisting of two proline-phenylalanine (PF) motifs: KPFRKLNPF. In contrast, despite EHD2 having nearly 70% amino acid identity with its paralogs, EHD1, EHD3 and EHD4, the latter proteins...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 25875965
DOI: 10.1371/journal.pone.0123710
PMCID: PMC4398442

Genes

EHD2
EHD1
EHD3
EHD4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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