Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions
Neuroglobin, a member of vertebrate globin family, is distributed primarily in the brain and retina. Considerable evidence has accumulated regarding its unique ligand-binding properties, neural-specific distribution, distinct expression regulation, and possible roles in processes such as neuron prot...
Published in: | Journal of Molecular Modeling |
---|---|
Main Authors: | , , , , |
Other Authors: | , , |
Format: | Journal/Newspaper |
Language: | English |
Published: |
journal of molecular modeling
2010
|
Subjects: | |
Online Access: | https://hdl.handle.net/20.500.11897/244159 https://doi.org/10.1007/s00894-009-0581-3 |
id |
ftpekinguniv:oai:localhost:20.500.11897/244159 |
---|---|
record_format |
openpolar |
spelling |
ftpekinguniv:oai:localhost:20.500.11897/244159 2023-05-15T18:26:50+02:00 Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions Xu, Jia Yin, Guowei Huang, Feijuan Wang, Baohuai Du, Weihong Du, WH (reprint author), Renmin Univ China, Dept Chem, Beijing 100872, Peoples R China. Renmin Univ China, Dept Chem, Beijing 100872, Peoples R China. Peking Univ, Inst Phys Chem, Beijing 100871, Peoples R China. 2010 https://hdl.handle.net/20.500.11897/244159 https://doi.org/10.1007/s00894-009-0581-3 en eng journal of molecular modeling JOURNAL OF MOLECULAR MODELING.2010,16,(4),759-770. 928580 1610-2940 http://hdl.handle.net/20.500.11897/244159 0948-5023 doi:10.1007/s00894-009-0581-3 WOS:000275122000013 SCI Molecular dynamics simulation Murine neuroglobin Mutants Proximal side NUCLEOTIDE DISSOCIATION INHIBITOR VERTEBRATE GLOBIN FAMILY LIGAND-BINDING AFFINITY SPERM-WHALE MYOGLOBIN HEXACOORDINATE HEMOGLOBIN OXYGEN-AFFINITY CYTOGLOBIN PROTEIN BRAIN NEURONS Journal 2010 ftpekinguniv https://doi.org/20.500.11897/244159 https://doi.org/10.1007/s00894-009-0581-3 2021-08-01T08:51:27Z Neuroglobin, a member of vertebrate globin family, is distributed primarily in the brain and retina. Considerable evidence has accumulated regarding its unique ligand-binding properties, neural-specific distribution, distinct expression regulation, and possible roles in processes such as neuron protection and enzymatic metabolism. Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding. In the present work, molecular dynamics (MD) simulations were employed to reveal functional and structural information in three carboxyl murine neuroglobin mutants with single point mutations F106Y, F106L and F106I, respectively. The MD simulation indicates a remarkable proximal effect on detectable displacement of heme and a larger tunnel in the protein matrix. In addition, the mutation at F106 confers on the CD region a very sensitive mobility in all three model structures. The dynamic features of neuroglobin demonstrate rearrangement of the inner space and highly active loop regions in solution. These imply that the conserved residue at the G5 site plays a key role in the physiological function of this unusual protein. http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000275122000013&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 Biochemistry & Molecular Biology Biophysics Chemistry, Multidisciplinary Computer Science, Interdisciplinary Applications SCI(E) 4 ARTICLE 4 759-770 16 Journal/Newspaper Sperm whale Peking University Institutional Repository (PKU IR) Journal of Molecular Modeling 16 4 759 770 |
institution |
Open Polar |
collection |
Peking University Institutional Repository (PKU IR) |
op_collection_id |
ftpekinguniv |
language |
English |
topic |
Molecular dynamics simulation Murine neuroglobin Mutants Proximal side NUCLEOTIDE DISSOCIATION INHIBITOR VERTEBRATE GLOBIN FAMILY LIGAND-BINDING AFFINITY SPERM-WHALE MYOGLOBIN HEXACOORDINATE HEMOGLOBIN OXYGEN-AFFINITY CYTOGLOBIN PROTEIN BRAIN NEURONS |
spellingShingle |
Molecular dynamics simulation Murine neuroglobin Mutants Proximal side NUCLEOTIDE DISSOCIATION INHIBITOR VERTEBRATE GLOBIN FAMILY LIGAND-BINDING AFFINITY SPERM-WHALE MYOGLOBIN HEXACOORDINATE HEMOGLOBIN OXYGEN-AFFINITY CYTOGLOBIN PROTEIN BRAIN NEURONS Xu, Jia Yin, Guowei Huang, Feijuan Wang, Baohuai Du, Weihong Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
topic_facet |
Molecular dynamics simulation Murine neuroglobin Mutants Proximal side NUCLEOTIDE DISSOCIATION INHIBITOR VERTEBRATE GLOBIN FAMILY LIGAND-BINDING AFFINITY SPERM-WHALE MYOGLOBIN HEXACOORDINATE HEMOGLOBIN OXYGEN-AFFINITY CYTOGLOBIN PROTEIN BRAIN NEURONS |
description |
Neuroglobin, a member of vertebrate globin family, is distributed primarily in the brain and retina. Considerable evidence has accumulated regarding its unique ligand-binding properties, neural-specific distribution, distinct expression regulation, and possible roles in processes such as neuron protection and enzymatic metabolism. Structurally, neuroglobin enjoys unique features, such as bis-histidyl coordination to heme iron in the absence of exogenous ligand, heme orientational heterogeneity, and a heme sliding mechanism accompanying ligand binding. In the present work, molecular dynamics (MD) simulations were employed to reveal functional and structural information in three carboxyl murine neuroglobin mutants with single point mutations F106Y, F106L and F106I, respectively. The MD simulation indicates a remarkable proximal effect on detectable displacement of heme and a larger tunnel in the protein matrix. In addition, the mutation at F106 confers on the CD region a very sensitive mobility in all three model structures. The dynamic features of neuroglobin demonstrate rearrangement of the inner space and highly active loop regions in solution. These imply that the conserved residue at the G5 site plays a key role in the physiological function of this unusual protein. http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000275122000013&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 Biochemistry & Molecular Biology Biophysics Chemistry, Multidisciplinary Computer Science, Interdisciplinary Applications SCI(E) 4 ARTICLE 4 759-770 16 |
author2 |
Du, WH (reprint author), Renmin Univ China, Dept Chem, Beijing 100872, Peoples R China. Renmin Univ China, Dept Chem, Beijing 100872, Peoples R China. Peking Univ, Inst Phys Chem, Beijing 100871, Peoples R China. |
format |
Journal/Newspaper |
author |
Xu, Jia Yin, Guowei Huang, Feijuan Wang, Baohuai Du, Weihong |
author_facet |
Xu, Jia Yin, Guowei Huang, Feijuan Wang, Baohuai Du, Weihong |
author_sort |
Xu, Jia |
title |
Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
title_short |
Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
title_full |
Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
title_fullStr |
Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
title_full_unstemmed |
Molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
title_sort |
molecular dynamics simulation of a carboxy murine neuroglobin mutated on the proximal side: heme displacement and concomitant rearrangement in loop regions |
publisher |
journal of molecular modeling |
publishDate |
2010 |
url |
https://hdl.handle.net/20.500.11897/244159 https://doi.org/10.1007/s00894-009-0581-3 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
SCI |
op_relation |
JOURNAL OF MOLECULAR MODELING.2010,16,(4),759-770. 928580 1610-2940 http://hdl.handle.net/20.500.11897/244159 0948-5023 doi:10.1007/s00894-009-0581-3 WOS:000275122000013 |
op_doi |
https://doi.org/20.500.11897/244159 https://doi.org/10.1007/s00894-009-0581-3 |
container_title |
Journal of Molecular Modeling |
container_volume |
16 |
container_issue |
4 |
container_start_page |
759 |
op_container_end_page |
770 |
_version_ |
1766208801896136704 |