1ebp

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spinqualitylabelsall models 1ebp, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

COMPLEX BETWEEN THE EXTRACELLULAR DOMAIN OF ERYTHROPOIETIN (EPO) RECEPTOR [EBP] AND AN AGONIST PEPTIDE [EMP1]

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The functional mimicry of a protein by an unrelated small molecule has, been a formidable challenge. Now, however, the biological activity of a, 166-residue hematopoietic growth hormone, erythropoietin (EPO), with its, class 1 cytokine receptor has been mimicked by a 20-residue cyclic peptide, unrelated in sequence to the natural ligand. The crystal structure at 2.8, A resolution of a complex of this agonist peptide with the extracellular, domain of EPO receptor reveals that a peptide dimer induces an almost, perfect twofold dimerization of the receptor. The dimer assembly differs, from that of the human growth hormone (hGH) receptor complex and suggests, that more than one mode of dimerization may be able to induce signal, transduction and cell proliferation. The EPO receptor binding site, defined by peptide interaction, corresponds to the smaller functional, epitope identified for hGH receptor. Similarly, the EPO mimetic peptide, ligand can be considered as a minimal hormone, and suggests the design of, nonpeptidic small molecule mimetics for EPO and other cytokines may indeed, be achievable.

Disease

Known disease associated with this structure: Erythrocytosis, familial OMIM:[133171]

About this Structure

1EBP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A., Livnah O, Stura EA, Johnson DL, Middleton SA, Mulcahy LS, Wrighton NC, Dower WJ, Jolliffe LK, Wilson IA, Science. 1996 Jul 26;273(5274):464-71. PMID:8662530

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