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The cryptochromes
Cryptochromes are photoreceptors that regulate entrainment by light of the circadian clock in plants and animals. They also act as integral parts of the central circadian oscillator in animal brains and as receptors controlling photomorphogenesis in response to blue or ultraviolet (UV-A) light in pl...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1175950/ https://www.ncbi.nlm.nih.gov/pubmed/15892880 http://dx.doi.org/10.1186/gb-2005-6-5-220 |
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author | Lin, Chentao Todo, Takeshi |
author_facet | Lin, Chentao Todo, Takeshi |
author_sort | Lin, Chentao |
collection | PubMed |
description | Cryptochromes are photoreceptors that regulate entrainment by light of the circadian clock in plants and animals. They also act as integral parts of the central circadian oscillator in animal brains and as receptors controlling photomorphogenesis in response to blue or ultraviolet (UV-A) light in plants. Cryptochromes are probably the evolutionary descendents of DNA photolyases, which are light-activated DNA-repair enzymes, and are classified into three groups - plant cryptochromes, animal cryptochromes, and CRY-DASH proteins. Cryptochromes and photolyases have similar three-dimensional structures, characterized by an α/β domain and a helical domain. The structure also includes a chromophore, flavin adenine dinucleotide (FAD). The FAD-access cavity of the helical domain is the catalytic site of photolyases, and it is predicted also to be important in the mechanism of cryptochromes. |
format | Text |
id | pubmed-1175950 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-11759502005-07-17 The cryptochromes Lin, Chentao Todo, Takeshi Genome Biol Protein Family Review Cryptochromes are photoreceptors that regulate entrainment by light of the circadian clock in plants and animals. They also act as integral parts of the central circadian oscillator in animal brains and as receptors controlling photomorphogenesis in response to blue or ultraviolet (UV-A) light in plants. Cryptochromes are probably the evolutionary descendents of DNA photolyases, which are light-activated DNA-repair enzymes, and are classified into three groups - plant cryptochromes, animal cryptochromes, and CRY-DASH proteins. Cryptochromes and photolyases have similar three-dimensional structures, characterized by an α/β domain and a helical domain. The structure also includes a chromophore, flavin adenine dinucleotide (FAD). The FAD-access cavity of the helical domain is the catalytic site of photolyases, and it is predicted also to be important in the mechanism of cryptochromes. BioMed Central 2005 2005-04-29 /pmc/articles/PMC1175950/ /pubmed/15892880 http://dx.doi.org/10.1186/gb-2005-6-5-220 Text en Copyright © 2005 BioMed Central Ltd |
spellingShingle | Protein Family Review Lin, Chentao Todo, Takeshi The cryptochromes |
title | The cryptochromes |
title_full | The cryptochromes |
title_fullStr | The cryptochromes |
title_full_unstemmed | The cryptochromes |
title_short | The cryptochromes |
title_sort | cryptochromes |
topic | Protein Family Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1175950/ https://www.ncbi.nlm.nih.gov/pubmed/15892880 http://dx.doi.org/10.1186/gb-2005-6-5-220 |
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