Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations
Neuroglobin (Ngb) is a heme protein, highly conserved along evolution, predominantly found in the nervous system. It is upregulated by hypoxia and ischemia and may have a neuroprotective role under hypoxic stress. Although many other roles have been proposed, the physiological function is still uncl...
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ftunibueairesbd:todo:paper_15216543_v63_n3_p206_Boron 2023-10-29T02:32:28+01:00 Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations Boron, I. Russo, R. Boechi, L. Cheng, C.-H.C. Di Prisco, G. Estrin, D.A. Verde, C. Nadra, A.D. https://hdl.handle.net/20.500.12110/paper_15216543_v63_n3_p206_Boron unknown http://hdl.handle.net/20.500.12110/paper_15216543_v63_n3_p206_Boron info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar evolution hemeproteins neuroglobin protein function protein structure structural biology amino terminal sequence Antarctica carboxy terminal sequence computer simulation conference paper fish gene sequence molecular dynamics mutation nonhuman nucleotide sequence protein analysis Amino Acid Sequence Animals Antarctic Regions Base Sequence DNA Primers Fishes Globins Molecular Dynamics Simulation Molecular Sequence Data Nerve Tissue Proteins Sequence Homology Amino Acid Chaenocephalus aceratus Dissostichus mawsoni Mammalia Salangini JOUR ftunibueairesbd https://doi.org/20.500.12110/paper_15216543_v63_n3_p206_Boron 2023-10-05T01:59:23Z Neuroglobin (Ngb) is a heme protein, highly conserved along evolution, predominantly found in the nervous system. It is upregulated by hypoxia and ischemia and may have a neuroprotective role under hypoxic stress. Although many other roles have been proposed, the physiological function is still unclear. Antarctic icefishes lack hemoglobin and some species also lack myoglobin, but all have Ngb and thus may help the elucidation of Ngb function. We present the first theoretically derived structure of fish Ngb and describe its behavior using molecular dynamics simulations. Specifically, we sequenced and analyzed Ngbs from a colorless-blooded Antarctic icefish species Chaenocephalus aceratus and a related red-blooded species (Dissostichus mawsoni). Both fish Ngbs are 6-coordinated but have some peculiarities that differentiate them from mammalian counterparts: they have extensions in the N and C termini that can interact with the EF loop, and a gap in the alignment that changes the CD-region structure/dynamics that has been found to play a key role in human neuroglobin. Our results suggest that a single mutation between both fish Ngbs is responsible for significant difference in the behavior of the proteins. The functional role of these characteristics is discussed. © 2011 IUBMB. Fil:Boechi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nadra, A.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Journal/Newspaper Antarc* Antarctic Antarctica Icefish Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
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Open Polar |
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Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
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ftunibueairesbd |
language |
unknown |
topic |
evolution hemeproteins neuroglobin protein function protein structure structural biology amino terminal sequence Antarctica carboxy terminal sequence computer simulation conference paper fish gene sequence molecular dynamics mutation nonhuman nucleotide sequence protein analysis Amino Acid Sequence Animals Antarctic Regions Base Sequence DNA Primers Fishes Globins Molecular Dynamics Simulation Molecular Sequence Data Nerve Tissue Proteins Sequence Homology Amino Acid Chaenocephalus aceratus Dissostichus mawsoni Mammalia Salangini |
spellingShingle |
evolution hemeproteins neuroglobin protein function protein structure structural biology amino terminal sequence Antarctica carboxy terminal sequence computer simulation conference paper fish gene sequence molecular dynamics mutation nonhuman nucleotide sequence protein analysis Amino Acid Sequence Animals Antarctic Regions Base Sequence DNA Primers Fishes Globins Molecular Dynamics Simulation Molecular Sequence Data Nerve Tissue Proteins Sequence Homology Amino Acid Chaenocephalus aceratus Dissostichus mawsoni Mammalia Salangini Boron, I. Russo, R. Boechi, L. Cheng, C.-H.C. Di Prisco, G. Estrin, D.A. Verde, C. Nadra, A.D. Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
topic_facet |
evolution hemeproteins neuroglobin protein function protein structure structural biology amino terminal sequence Antarctica carboxy terminal sequence computer simulation conference paper fish gene sequence molecular dynamics mutation nonhuman nucleotide sequence protein analysis Amino Acid Sequence Animals Antarctic Regions Base Sequence DNA Primers Fishes Globins Molecular Dynamics Simulation Molecular Sequence Data Nerve Tissue Proteins Sequence Homology Amino Acid Chaenocephalus aceratus Dissostichus mawsoni Mammalia Salangini |
description |
Neuroglobin (Ngb) is a heme protein, highly conserved along evolution, predominantly found in the nervous system. It is upregulated by hypoxia and ischemia and may have a neuroprotective role under hypoxic stress. Although many other roles have been proposed, the physiological function is still unclear. Antarctic icefishes lack hemoglobin and some species also lack myoglobin, but all have Ngb and thus may help the elucidation of Ngb function. We present the first theoretically derived structure of fish Ngb and describe its behavior using molecular dynamics simulations. Specifically, we sequenced and analyzed Ngbs from a colorless-blooded Antarctic icefish species Chaenocephalus aceratus and a related red-blooded species (Dissostichus mawsoni). Both fish Ngbs are 6-coordinated but have some peculiarities that differentiate them from mammalian counterparts: they have extensions in the N and C termini that can interact with the EF loop, and a gap in the alignment that changes the CD-region structure/dynamics that has been found to play a key role in human neuroglobin. Our results suggest that a single mutation between both fish Ngbs is responsible for significant difference in the behavior of the proteins. The functional role of these characteristics is discussed. © 2011 IUBMB. Fil:Boechi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nadra, A.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
format |
Journal/Newspaper |
author |
Boron, I. Russo, R. Boechi, L. Cheng, C.-H.C. Di Prisco, G. Estrin, D.A. Verde, C. Nadra, A.D. |
author_facet |
Boron, I. Russo, R. Boechi, L. Cheng, C.-H.C. Di Prisco, G. Estrin, D.A. Verde, C. Nadra, A.D. |
author_sort |
Boron, I. |
title |
Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
title_short |
Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
title_full |
Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
title_fullStr |
Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
title_full_unstemmed |
Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
title_sort |
structure and dynamics of antarctic fish neuroglobin assessed by computer simulations |
url |
https://hdl.handle.net/20.500.12110/paper_15216543_v63_n3_p206_Boron |
genre |
Antarc* Antarctic Antarctica Icefish |
genre_facet |
Antarc* Antarctic Antarctica Icefish |
op_relation |
http://hdl.handle.net/20.500.12110/paper_15216543_v63_n3_p206_Boron |
op_rights |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
op_doi |
https://doi.org/20.500.12110/paper_15216543_v63_n3_p206_Boron |
_version_ |
1781053951146196992 |