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Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation
Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein mo...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Biophysical Society of Japan (BSJ)
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736795/ https://www.ncbi.nlm.nih.gov/pubmed/27493522 http://dx.doi.org/10.2142/biophysics.11.103 |
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author | Yanaka, Saeko Ueno, Takamasa Tsumoto, Kouhei Sugase, Kenji |
author_facet | Yanaka, Saeko Ueno, Takamasa Tsumoto, Kouhei Sugase, Kenji |
author_sort | Yanaka, Saeko |
collection | PubMed |
description | Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins. |
format | Online Article Text |
id | pubmed-4736795 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
spelling | pubmed-47367952016-08-04 Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation Yanaka, Saeko Ueno, Takamasa Tsumoto, Kouhei Sugase, Kenji Biophysics (Nagoya-shi) Review Article Structural fluctuation on microsecond to millisecond time scales has been reported to play an important role in proteins that undergo significant structural change during their expression of function. In these proteins, the structural change was obvious in the crystal structures. However, protein motions in solution could contribute to the function of proteins, even if no significant structural difference is observed in crystal structure of different states while they function. In this review, we introduce our recent report on the stabilization mechanism of human leukocyte antigen, and the possibility of fluctuation contributing to several biophysical properties of proteins. The Biophysical Society of Japan (BSJ) 2015-04-18 /pmc/articles/PMC4736795/ /pubmed/27493522 http://dx.doi.org/10.2142/biophysics.11.103 Text en 2015 © The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Yanaka, Saeko Ueno, Takamasa Tsumoto, Kouhei Sugase, Kenji Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title | Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title_full | Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title_fullStr | Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title_full_unstemmed | Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title_short | Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
title_sort | revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4736795/ https://www.ncbi.nlm.nih.gov/pubmed/27493522 http://dx.doi.org/10.2142/biophysics.11.103 |
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