ᱨᱮᱫ:Serpin equilibrium.png
ᱧᱮᱞᱡᱚᱝ ᱨᱮᱱᱟᱜ ᱟᱠᱟᱨ:᱘᱐᱐ × ᱕᱐᱗ ᱯᱤᱠᱥᱮᱞ ᱮᱴᱟᱜ ᱨᱤᱡᱚᱞᱩᱥᱚᱱᱥ: ᱓᱒᱐ × ᱒᱐᱓ ᱯᱤᱠᱥᱮᱞ | ᱖᱔᱐ × ᱔᱐᱖ ᱯᱤᱠᱥᱮᱞ | ᱑,᱐᱒᱔ × ᱖᱔᱙ ᱯᱤᱠᱥᱮᱞ | ᱑,᱒᱘᱐ × ᱘᱑᱒ ᱯᱤᱠᱥᱮᱞ | ᱓,᱐᱐᱐ × ᱑,᱙᱐᱒ ᱯᱤᱠᱥᱮᱞ
ᱟᱥᱚᱞ ᱨᱮᱫ (᱓,᱐᱐᱐ x ᱑,᱙᱐᱒ pixels, file size: ᱑.᱔᱑ MB, MIME type: image/png)
ᱢᱩᱬᱩᱛ ᱠᱟᱛᱷᱟ
| ᱵᱤᱵᱚᱨᱚᱱᱤ |
English: The native state of serpins is an equilibrium between a fully-stressed state (left) and a partially relaxed state (right). The five-stranded A-sheet (light blue) contains two functionally important regions for the serpin's mechanism, the breach and the shutter. The Reactive Centre Loop (RCL, blue) exists in a dynamic equilibrium between the fully exposed conformation (left) and a conformation where it is partially inserted into the breach of the A-sheet (right). (PDB: 1QLP, 1YXA).
[1] [2] |
| ᱢᱟᱹᱦᱤᱛ | |
| ᱯᱷᱮᱰᱟᱛ | ᱤᱧᱟᱜ ᱠᱟᱹᱢᱤ |
| ᱚᱱᱚᱞᱤᱭᱟᱹ | Thomas Shafee |
ᱞᱟᱭᱥᱮᱱᱥ ᱛᱮᱭᱟᱨ
I, the copyright holder of this work, hereby publish it under the following license:
This file is licensed under the Creative Commons Attribution 4.0 International license.
- ᱟᱲᱟᱜ ᱜᱮᱭᱟᱢ:
- ᱦᱟᱹᱴᱤᱧᱢᱮ – ᱱᱚᱠᱚᱞ ᱞᱟᱹᱜᱤᱫ, ᱦᱟᱹᱴᱤᱧ ᱟᱨ ᱵᱷᱮᱡᱟᱭᱢᱮ ᱠᱟᱹᱢᱤ
- ᱢᱮᱥᱟᱣᱠᱟᱛᱢᱮ – ᱠᱟᱹᱢᱤ ᱟᱞᱜᱟᱭ ᱞᱟᱹᱜᱤᱫ
- ᱞᱟᱛᱟᱨ ᱨᱮᱭᱟᱜ ᱨᱤᱛ ᱞᱮᱠᱟᱛᱮ:
- ᱟᱴᱨᱤᱵᱩᱥᱚᱱ – ᱟᱢ ᱠᱟᱹᱢᱤ ᱥᱚᱫᱚᱨ ᱦᱩᱭᱟᱢᱟ ᱡᱚᱠᱷᱚᱱ ᱚᱱᱚᱞᱤᱭᱟᱹ ᱟᱨᱵᱟᱝ ᱞᱟᱭᱥᱮᱸᱥᱩᱭᱟᱹ ᱫᱟᱨᱟᱭᱛᱮ ᱠᱟᱛᱷᱟ ᱨᱟᱠᱟᱵ ᱠᱷᱟᱱ (ᱢᱮᱱᱠᱷᱟᱱ ᱟᱠᱚ ᱩᱫᱩᱜᱟᱜ ᱦᱚᱨ ᱛᱮᱫᱚ ᱵᱟᱝ ᱡᱟᱦᱟᱸ ᱟᱠᱚᱠᱚ ᱜᱚᱲᱚᱣᱟᱢ ᱟᱨᱵᱟᱝ ᱟᱢᱟᱜ ᱠᱟᱹᱢᱤ ᱨᱮᱱᱟᱜ ᱵᱮᱵᱷᱟᱨ)
- ↑ Elliott PR, Lomas DA, Carrell RW, Abrahams JP. (1996). "Inhibitory conformation of the reactive loop of alpha 1-antitrypsin". Nature Structural & Molecular Biology 3 (8): 676–81. DOI:10.1038/nsb0896-676. PMID 8756325.
- ↑ (2005). "The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins.". J Biol Chem 280 (52): 43168–78. DOI:10.1074/jbc.M505598200. PMID 16141197.
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