1QJT

SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15

Summary for 1QJT

• Entry DOI: 10.2210/pdb1qjt/pdb
• NMR Information: BMRB: 4491
• Descriptor: EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE SUBSTRATE 15, EPS15 (1 entity in total)
• Functional Keywords: growth factor, eh domain, eps15, ef-hand, solution structure, s100 protein
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 1
• Total formula weight: 10672.21

Authors

Whitehead, B.,Tessari, M.,Carotenuto, A.,van Bergen en Henegouwen, P.M.,Vuister, G.W. (deposition date: 1999-07-02, release date: 2000-01-23, Last modification date: 2024-05-15)

Primary citation

Whitehead, B.,Tessari, M.,Carotenuto, A.,van Bergen en Henegouwen, P.M.,Vuister, G.W.
The Eh1 Domain of Eps15 is Structurally Classified as a Member of the S100 Subclass of EF-Hand Containing Proteins
Biochemistry, 38:11271-11277, 1999

PubMed Abstract: The Eps15 homology (EH) domain is a protein-protein interaction module that binds to proteins containing the asparagine-proline-phenylalanine (NPF) or tryptophan/phenylalanine-tryptophan (W/FW) motif. EH domain-containing proteins serve important roles in signaling and processes connected to transport, protein sorting, and organization of subcellular structure. Here, we report the solution structure of the apo form of the EH1 domain of mouse Eps15, as determined by high-resolution multidimensional heteronuclear NMR spectroscopy. The polypeptide folds into six alpha-helices and a short antiparallel beta-sheet. Additionally, it contains a long, structured, topologically unique C-terminal loop. Helices 2-5 form two EF-hand motifs. Structural similarity and Ca(2+) binding properties lead to classification of the EH1 domain as a member of the S100 subclass of EF-hand-containing proteins, albeit with a unique set of interhelical angles. Binding studies using an eight-residue NPF-containing peptide derived from RAB, the cellular cofactor of the HIV Rev protein, show a hydrophobic peptide-binding pocket formed by conserved tryptophan and leucine residues.

PubMed: 10471276
DOI: 10.1021/BI990922I

Experimental method

SOLUTION NMR