1y3k

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Revision as of 18:08, 12 November 2007

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Solution structure of the apo form of the fifth domain of Menkes protein

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The interaction between the human copper(I) chaperone, HAH1, and one of, its two physiological partners, the Menkes disease protein (ATP7A), was, investigated in solution using heteronuclear NMR. The study was carried, out through titrations involving HAH1 and either the second or the fifth, soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of, copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast, homologous system. In particular, no stable adduct is formed between, either of the MNK domains and HAH1. The copper(I) transfer reaction is, slow on the time scale of the NMR chemical shift, and the equilibrium is, significantly shifted towards the formation of copper(I)-MNK2/MNK5. The, solution structures of both apo- and copper(I)-MNK5, which were not, available, are also reported. The results are discussed in comparison with, the data available in the literature for the interaction between HAH1 and, its partners from other spectroscopic techniques.

Disease

Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific OMIM:[155555], Blond/light brown hair and/or fair skin OMIM:[155555], Cutis laxa, neonatal OMIM:[300011], Melanoma, susceptiblity to OMIM:[155555], Menkes disease OMIM:[300011], Occipital horn syndrome OMIM:[300011], Oculocutaneous albinism, type II, modifier of OMIM:[155555], Red hair/fair skin OMIM:[155555], UV-induced skin damage, susceptibility to OMIM:[155555]

About this Structure

1Y3K is a Single protein structure of sequence from Homo sapiens. Active as Copper-exporting ATPase, with EC number 3.6.3.4 Full crystallographic information is available from OCA.

Reference

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein., Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A, FEBS J. 2005 Feb;272(3):865-71. PMID:15670166

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