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Article

Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.

Science (New York, N.Y.) - 28 Aug 1998

de Beer T, Carter R E, Lobel-Rice K E, Sorkin A, Overduin M

Abstract excerpt

Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second...

Topics

Amino Acid Sequence
Binding Sites
Calcium
Calcium-Binding Proteins
Helix-Loop-Helix Motifs
Ligands
Models, Molecular
Molecular Sequence Data
Mutation
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides
Phosphoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Protein Folding

Protein Structure, Secondary

Signal Transduction

Source

Identifiers

PMID: 9721102
DOI: 10.1126/science.281.5381.1357

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9721102-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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