1yju

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(New page: 200px<br /> <applet load="1yju" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yju" /> '''Solution structure of the apo form of the s...)
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'''Solution structure of the apo form of the sixth soluble domain of Menkes protein'''<br />
'''Solution structure of the apo form of the sixth soluble domain of Menkes protein'''<br />
==Overview==
==Overview==
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Menkes disease is a fatal disease that can be induced by various mutations, in the ATP7A gene, leading to unpaired uptake of dietary copper. The ATP7A, gene encodes a copper(I)-translocating ATPase. Here the disease-causing, A629P mutation, which occurs in the last of the six copper(I)-binding, soluble domains of the ATPase (hereafter MNK6), was investigated. To, understand why this apparently minor amino acid replacement is pathogenic, the solution structures and dynamics on various time-scales of wild-type, and A629P-MNK6 were determined both in the apo- and copper(I)-loaded, forms. The interaction in vitro with the physiological ATP7A, copper(I)-donor (HAH1) was additionally studied. The A629P mutation makes, the protein beta-sheet more solvent accessible, possibly resulting in an, enhanced susceptibility of ATP7A to proteolytic cleavage and/or in reduced, capability of copper(I)-translocation. A small reduction of the affinity, for copper(I) is also observed. Both effects could concur to, pathogenicity.
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Menkes disease is a fatal disease that can be induced by various mutations in the ATP7A gene, leading to unpaired uptake of dietary copper. The ATP7A gene encodes a copper(I)-translocating ATPase. Here the disease-causing A629P mutation, which occurs in the last of the six copper(I)-binding soluble domains of the ATPase (hereafter MNK6), was investigated. To understand why this apparently minor amino acid replacement is pathogenic, the solution structures and dynamics on various time-scales of wild-type and A629P-MNK6 were determined both in the apo- and copper(I)-loaded forms. The interaction in vitro with the physiological ATP7A copper(I)-donor (HAH1) was additionally studied. The A629P mutation makes the protein beta-sheet more solvent accessible, possibly resulting in an enhanced susceptibility of ATP7A to proteolytic cleavage and/or in reduced capability of copper(I)-translocation. A small reduction of the affinity for copper(I) is also observed. Both effects could concur to pathogenicity.
==Disease==
==Disease==
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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]], Blond/light brown hair and/or fair skin 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, susceptiblity 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]], Red hair/fair skin OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]], UV-induced skin damage, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155555 155555]]
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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==
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1YJU 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YJU OCA].
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1YJU 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=1YJU OCA].
==Reference==
==Reference==
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[[Category: Migliardi, M.]]
[[Category: Migliardi, M.]]
[[Category: Rosato, A.]]
[[Category: Rosato, A.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Wang, S.]]
[[Category: Wang, S.]]
[[Category: copper(i)]]
[[Category: copper(i)]]
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[[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 16:06:04 2008''

Revision as of 14:06, 21 February 2008


1yju

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Solution structure of the apo form of the sixth soluble domain of Menkes protein

Contents

Overview

Menkes disease is a fatal disease that can be induced by various mutations in the ATP7A gene, leading to unpaired uptake of dietary copper. The ATP7A gene encodes a copper(I)-translocating ATPase. Here the disease-causing A629P mutation, which occurs in the last of the six copper(I)-binding soluble domains of the ATPase (hereafter MNK6), was investigated. To understand why this apparently minor amino acid replacement is pathogenic, the solution structures and dynamics on various time-scales of wild-type and A629P-MNK6 were determined both in the apo- and copper(I)-loaded forms. The interaction in vitro with the physiological ATP7A copper(I)-donor (HAH1) was additionally studied. The A629P mutation makes the protein beta-sheet more solvent accessible, possibly resulting in an enhanced susceptibility of ATP7A to proteolytic cleavage and/or in reduced capability of copper(I)-translocation. A small reduction of the affinity for copper(I) is also observed. Both effects could concur to pathogenicity.

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

1YJU 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 atomic-level investigation of the disease-causing A629P mutant of the Menkes protein, ATP7A., Banci L, Bertini I, Cantini F, Migliardi M, Rosato A, Wang S, J Mol Biol. 2005 Sep 16;352(2):409-17. PMID:16083905

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