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CBS domains: structure, function, and pathology in human proteins
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| Zeitschriftentitel: | American Journal of Physiology-Cell Physiology |
|---|---|
| Personen und Körperschaften: | , |
| In: | American Journal of Physiology-Cell Physiology, 289, 2005, 6, S. C1369-C1378 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Physiological Society
|
| Schlagwörter: |
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Ignoul, Sofie Eggermont, Jan Ignoul, Sofie Eggermont, Jan |
|---|---|
| author |
Ignoul, Sofie Eggermont, Jan |
| spellingShingle |
Ignoul, Sofie Eggermont, Jan American Journal of Physiology-Cell Physiology CBS domains: structure, function, and pathology in human proteins Cell Biology Physiology |
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ignoul, sofie |
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Ignoul, Sofie Eggermont, Jan 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00282.2005 <jats:p>The cystathionine-β-synthase (CBS) domain is an evolutionarily conserved protein domain that is present in the proteome of archaebacteria, prokaryotes, and eukaryotes. CBS domains usually come in tandem repeats and are found in cytosolic and membrane proteins performing different functions (metabolic enzymes, kinases, and channels). Crystallographic studies of bacterial CBS domains have shown that two CBS domains form an intramolecular dimeric structure (CBS pair). Several human hereditary diseases (homocystinuria, retinitis pigmentosa, hypertrophic cardiomyopathy, myotonia congenital, etc.) can be caused by mutations in CBS domains of, respectively, cystathionine-β-synthase, inosine 5′-monophosphate dehydrogenase, AMP kinase, and chloride channels. Despite their clinical relevance, it remains to be established what the precise function of CBS domains is and how they affect the structural and/or functional properties of an enzyme, kinase, or channel. Depending on the protein in which they occur, CBS domains have been proposed to affect multimerization and sorting of proteins, channel gating, and ligand binding. However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.</jats:p> CBS domains: structure, function, and pathology in human proteins American Journal of Physiology-Cell Physiology |
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CBS domains: structure, function, and pathology in human proteins |
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CBS domains: structure, function, and pathology in human proteins |
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CBS domains: structure, function, and pathology in human proteins |
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CBS domains: structure, function, and pathology in human proteins |
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CBS domains: structure, function, and pathology in human proteins |
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CBS domains: structure, function, and pathology in human proteins |
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cbs domains: structure, function, and pathology in human proteins |
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Cell Biology Physiology |
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http://dx.doi.org/10.1152/ajpcell.00282.2005 |
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2005 |
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C1369-C1378 |
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<jats:p>The cystathionine-β-synthase (CBS) domain is an evolutionarily conserved protein domain that is present in the proteome of archaebacteria, prokaryotes, and eukaryotes. CBS domains usually come in tandem repeats and are found in cytosolic and membrane proteins performing different functions (metabolic enzymes, kinases, and channels). Crystallographic studies of bacterial CBS domains have shown that two CBS domains form an intramolecular dimeric structure (CBS pair). Several human hereditary diseases (homocystinuria, retinitis pigmentosa, hypertrophic cardiomyopathy, myotonia congenital, etc.) can be caused by mutations in CBS domains of, respectively, cystathionine-β-synthase, inosine 5′-monophosphate dehydrogenase, AMP kinase, and chloride channels. Despite their clinical relevance, it remains to be established what the precise function of CBS domains is and how they affect the structural and/or functional properties of an enzyme, kinase, or channel. Depending on the protein in which they occur, CBS domains have been proposed to affect multimerization and sorting of proteins, channel gating, and ligand binding. However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.</jats:p> |
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| description | <jats:p>The cystathionine-β-synthase (CBS) domain is an evolutionarily conserved protein domain that is present in the proteome of archaebacteria, prokaryotes, and eukaryotes. CBS domains usually come in tandem repeats and are found in cytosolic and membrane proteins performing different functions (metabolic enzymes, kinases, and channels). Crystallographic studies of bacterial CBS domains have shown that two CBS domains form an intramolecular dimeric structure (CBS pair). Several human hereditary diseases (homocystinuria, retinitis pigmentosa, hypertrophic cardiomyopathy, myotonia congenital, etc.) can be caused by mutations in CBS domains of, respectively, cystathionine-β-synthase, inosine 5′-monophosphate dehydrogenase, AMP kinase, and chloride channels. Despite their clinical relevance, it remains to be established what the precise function of CBS domains is and how they affect the structural and/or functional properties of an enzyme, kinase, or channel. Depending on the protein in which they occur, CBS domains have been proposed to affect multimerization and sorting of proteins, channel gating, and ligand binding. However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.</jats:p> |
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| spelling | Ignoul, Sofie Eggermont, Jan 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.00282.2005 <jats:p>The cystathionine-β-synthase (CBS) domain is an evolutionarily conserved protein domain that is present in the proteome of archaebacteria, prokaryotes, and eukaryotes. CBS domains usually come in tandem repeats and are found in cytosolic and membrane proteins performing different functions (metabolic enzymes, kinases, and channels). Crystallographic studies of bacterial CBS domains have shown that two CBS domains form an intramolecular dimeric structure (CBS pair). Several human hereditary diseases (homocystinuria, retinitis pigmentosa, hypertrophic cardiomyopathy, myotonia congenital, etc.) can be caused by mutations in CBS domains of, respectively, cystathionine-β-synthase, inosine 5′-monophosphate dehydrogenase, AMP kinase, and chloride channels. Despite their clinical relevance, it remains to be established what the precise function of CBS domains is and how they affect the structural and/or functional properties of an enzyme, kinase, or channel. Depending on the protein in which they occur, CBS domains have been proposed to affect multimerization and sorting of proteins, channel gating, and ligand binding. However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.</jats:p> CBS domains: structure, function, and pathology in human proteins American Journal of Physiology-Cell Physiology |
| spellingShingle | Ignoul, Sofie, Eggermont, Jan, American Journal of Physiology-Cell Physiology, CBS domains: structure, function, and pathology in human proteins, Cell Biology, Physiology |
| title | CBS domains: structure, function, and pathology in human proteins |
| title_full | CBS domains: structure, function, and pathology in human proteins |
| title_fullStr | CBS domains: structure, function, and pathology in human proteins |
| title_full_unstemmed | CBS domains: structure, function, and pathology in human proteins |
| title_short | CBS domains: structure, function, and pathology in human proteins |
| title_sort | cbs domains: structure, function, and pathology in human proteins |
| title_unstemmed | CBS domains: structure, function, and pathology in human proteins |
| topic | Cell Biology, Physiology |
| url | http://dx.doi.org/10.1152/ajpcell.00282.2005 |