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Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain
Ficolins are pathogen-recognition molecules in innate immune systems. The crystal structure of the human M-ficolin recognition domain (FD1) has been determined at 1.9 Å resolution, and compared with that of the human fibrinogen γ fragment, tachylectin-5A, L-ficolin and H-ficolin. The overall structu...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394802/ https://www.ncbi.nlm.nih.gov/pubmed/18421149 http://dx.doi.org/10.1107/S0909049507054325 |
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author | Tanio, Michikazu Kondo, Shin Sugio, Shigetoshi Kohno, Toshiyuki |
author_facet | Tanio, Michikazu Kondo, Shin Sugio, Shigetoshi Kohno, Toshiyuki |
author_sort | Tanio, Michikazu |
collection | PubMed |
description | Ficolins are pathogen-recognition molecules in innate immune systems. The crystal structure of the human M-ficolin recognition domain (FD1) has been determined at 1.9 Å resolution, and compared with that of the human fibrinogen γ fragment, tachylectin-5A, L-ficolin and H-ficolin. The overall structure of FD1 is similar to that of the other proteins, although the peptide bond between Asp282 and Cys283, which is in a predicted ligand-binding site, is a normal trans bond, unlike the cases of the other proteins. Analysis of the pH-dependent ligand-binding activity of FD1 in solution suggested that a conformational equilibrium between active and non-active forms in the ligand-binding region, involving cis-trans isomerization of the Asp282—Cys283 peptide bond, contributes to the discrimination between self and non-self, and that the pK (a) values of His284 are 6.1 and 6.3 in the active and non-active forms, respectively. |
format | Text |
id | pubmed-2394802 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-23948022009-03-05 Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain Tanio, Michikazu Kondo, Shin Sugio, Shigetoshi Kohno, Toshiyuki J Synchrotron Radiat Diffraction Structural Biology Ficolins are pathogen-recognition molecules in innate immune systems. The crystal structure of the human M-ficolin recognition domain (FD1) has been determined at 1.9 Å resolution, and compared with that of the human fibrinogen γ fragment, tachylectin-5A, L-ficolin and H-ficolin. The overall structure of FD1 is similar to that of the other proteins, although the peptide bond between Asp282 and Cys283, which is in a predicted ligand-binding site, is a normal trans bond, unlike the cases of the other proteins. Analysis of the pH-dependent ligand-binding activity of FD1 in solution suggested that a conformational equilibrium between active and non-active forms in the ligand-binding region, involving cis-trans isomerization of the Asp282—Cys283 peptide bond, contributes to the discrimination between self and non-self, and that the pK (a) values of His284 are 6.1 and 6.3 in the active and non-active forms, respectively. International Union of Crystallography 2008-05-01 2008-04-18 /pmc/articles/PMC2394802/ /pubmed/18421149 http://dx.doi.org/10.1107/S0909049507054325 Text en © International Union of Crystallography 2008 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Diffraction Structural Biology Tanio, Michikazu Kondo, Shin Sugio, Shigetoshi Kohno, Toshiyuki Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title | Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title_full | Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title_fullStr | Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title_full_unstemmed | Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title_short | Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain |
title_sort | trimeric structure and conformational equilibrium of m-ficolin fibrinogen-like domain |
topic | Diffraction Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394802/ https://www.ncbi.nlm.nih.gov/pubmed/18421149 http://dx.doi.org/10.1107/S0909049507054325 |
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