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231223s2008 xx |||||o 00| ||eng c |
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|a 10.1107/S0909049507054325
|2 doi
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|a pubmed24n1222.xml
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|a (DE-627)NLM179010972
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|a (NLM)18421149
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Tanio, Michikazu
|e verfasserin
|4 aut
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| 245 |
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|a Trimeric structure and conformational equilibrium of M-ficolin fibrinogen-like domain
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 31.07.2008
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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 A resolution, and compared with that of the human fibrinogen gamma 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
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Biopolymers
|2 NLM
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| 650 |
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|a Lectins
|2 NLM
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| 650 |
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|a Fibrinogen
|2 NLM
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| 650 |
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|a 9001-32-5
|2 NLM
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| 700 |
1 |
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|a Kondo, Shin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sugio, Shigetoshi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kohno, Toshiyuki
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 15(2008), Pt 3 vom: 07. Mai, Seite 243-5
|w (DE-627)NLM09824129X
|x 1600-5775
|7 nnns
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| 773 |
1 |
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|g volume:15
|g year:2008
|g number:Pt 3
|g day:07
|g month:05
|g pages:243-5
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|u http://dx.doi.org/10.1107/S0909049507054325
|3 Volltext
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|a GBV_ILN_2005
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|a AR
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|d 15
|j 2008
|e Pt 3
|b 07
|c 05
|h 243-5
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