1qjt
From Proteopedia
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SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15
Overview
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.
About this Structure
1QJT is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins., Whitehead B, Tessari M, Carotenuto A, van Bergen en Henegouwen PM, Vuister GW, Biochemistry. 1999 Aug 31;38(35):11271-7. PMID:10471276
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