1y3k

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[[Image:1y3k.gif|left|200px]]<br /><applet load="1y3k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y3k.gif|left|200px]]
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caption="1y3k" />
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'''Solution structure of the apo form of the fifth domain of Menkes protein'''<br />
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{{Structure
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|PDB= 1y3k |SIZE=350|CAPTION= <scene name='initialview01'>1y3k</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4]
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|GENE= ATP7A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Solution structure of the apo form of the fifth domain of Menkes protein'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3K OCA].
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1Y3K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3K OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15670166 15670166]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15670166 15670166]
[[Category: Copper-exporting ATPase]]
[[Category: Copper-exporting ATPase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: ferrodoxin-like fold]]
[[Category: ferrodoxin-like fold]]
[[Category: spine]]
[[Category: spine]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:01 2008''

Revision as of 13:18, 20 March 2008


PDB ID 1y3k

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Gene: ATP7A (Homo sapiens)
Activity: Copper-exporting ATPase, with EC number 3.6.3.4
Coordinates: save as pdb, mmCIF, xml



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 diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific , OMIM:[155555], Cutis laxa, neonatal OMIM:[300011], Melanoma susceptibility to OMIM:[155555], Menkes disease OMIM:[300011], Occipital horn syndrome OMIM:[300011], Oculocutaneous albinism, type II, modifier of OMIM:[155555], Skin/hair/eye pigmentation 2, blond hair/fair skin OMIM:[155555], Skin/hair/eye pigmentation 2, red hair/fair skin OMIM:[155555], UV-induced skin damage OMIM:[155555]

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

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