1y3k
From Proteopedia
(New page: 200px<br /> <applet load="1y3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y3k" /> '''Solution structure of the apo form of the f...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1y3k.gif|left|200px]]<br /> | + | [[Image:1y3k.gif|left|200px]]<br /><applet load="1y3k" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1y3k" size=" | + | |
caption="1y3k" /> | caption="1y3k" /> | ||
'''Solution structure of the apo form of the fifth domain of Menkes protein'''<br /> | '''Solution structure of the apo form of the fifth domain of Menkes protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The interaction between the human copper(I) chaperone, HAH1, and one of | + | 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== | ==Disease== | ||
| - | Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], | + | Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific , OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Cutis laxa, neonatal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Melanoma susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Menkes disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Occipital horn syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300011 300011]], Oculocutaneous albinism, type II, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Skin/hair/eye pigmentation 2, blond hair/fair skin OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], Skin/hair/eye pigmentation 2, red hair/fair skin OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], UV-induced skin damage OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]] |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 18: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Banci, L.]] | [[Category: Banci, L.]] | ||
| - | [[Category: Chasapis, C | + | [[Category: Chasapis, C T.]] |
[[Category: Ciofi-Baffoni, S.]] | [[Category: Ciofi-Baffoni, S.]] | ||
[[Category: Hadjiliadis, N.]] | [[Category: Hadjiliadis, N.]] | ||
[[Category: Rosato, A.]] | [[Category: Rosato, A.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: beta-alpha-beta-beta-alpha-beta structure]] | [[Category: beta-alpha-beta-beta-alpha-beta structure]] | ||
[[Category: ferrodoxin-like fold]] | [[Category: ferrodoxin-like fold]] | ||
| Line 30: | Line 29: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:27 2008'' |
Revision as of 14:01, 21 February 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 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. 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
Page seeded by OCA on Thu Feb 21 16:01:27 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 genomics | Structural proteomics in europe
