1y3k
From Proteopedia
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'''Solution structure of the apo form of the fifth domain of Menkes protein''' | '''Solution structure of the apo form of the fifth domain of Menkes protein''' | ||
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[[Category: Rosato, A.]] | [[Category: Rosato, A.]] | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
| - | [[Category: | + | [[Category: Beta-alpha-beta-beta-alpha-beta structure]] |
| - | [[Category: | + | [[Category: Ferrodoxin-like fold]] |
| - | [[Category: | + | [[Category: Spine]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structural proteomics in europe]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:14:50 2008'' | |
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Revision as of 05:14, 13 April 2008
Solution structure of the apo form of the fifth domain of Menkes protein
Contents |
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 disease associated with this structure: Cutis laxa, neonatal OMIM:[300011], Menkes disease OMIM:[300011], Occipital horn syndrome OMIM:[300011]
About this Structure
1Y3K is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sun Apr 13 08:14:50 2008
Categories: Copper-exporting ATPase | Homo sapiens | Single protein | Banci, L. | Chasapis, C T. | Ciofi-Baffoni, S. | Hadjiliadis, N. | Rosato, A. | SPINE, Structural Proteomics in Europe. | Beta-alpha-beta-beta-alpha-beta structure | Ferrodoxin-like fold | Spine | Structural genomic | Structural proteomics in europe
