Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations
Abstract 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 s...
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crwiley:10.1002/iub.444 2024-06-02T07:57:46+00:00 Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations Boron, Ignacio Russo, Roberta Boechi, Leonardo Cheng, C.‐H. Christina di Prisco, Guido Estrin, Darío A. Verde, Cinzia Nadra, Alejandro D. 2011 http://dx.doi.org/10.1002/iub.444 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.444 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.444 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor IUBMB Life volume 63, issue 3, page 206-213 ISSN 1521-6543 1521-6551 journal-article 2011 crwiley https://doi.org/10.1002/iub.444 2024-05-03T11:57:06Z Abstract 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 IUBMB Life, 63(3): 206–213, 2011 Article in Journal/Newspaper Antarc* Antarctic Icefish Wiley Online Library Antarctic IUBMB Life 63 3 206 213 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract 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 IUBMB Life, 63(3): 206–213, 2011 |
format |
Article in Journal/Newspaper |
author |
Boron, Ignacio Russo, Roberta Boechi, Leonardo Cheng, C.‐H. Christina di Prisco, Guido Estrin, Darío A. Verde, Cinzia Nadra, Alejandro D. |
spellingShingle |
Boron, Ignacio Russo, Roberta Boechi, Leonardo Cheng, C.‐H. Christina di Prisco, Guido Estrin, Darío A. Verde, Cinzia Nadra, Alejandro D. Structure and dynamics of Antarctic fish neuroglobin assessed by computer simulations |
author_facet |
Boron, Ignacio Russo, Roberta Boechi, Leonardo Cheng, C.‐H. Christina di Prisco, Guido Estrin, Darío A. Verde, Cinzia Nadra, Alejandro D. |
author_sort |
Boron, Ignacio |
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 |
publisher |
Wiley |
publishDate |
2011 |
url |
http://dx.doi.org/10.1002/iub.444 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.444 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.444 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_source |
IUBMB Life volume 63, issue 3, page 206-213 ISSN 1521-6543 1521-6551 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/iub.444 |
container_title |
IUBMB Life |
container_volume |
63 |
container_issue |
3 |
container_start_page |
206 |
op_container_end_page |
213 |
_version_ |
1800740961301561344 |