File:Serpin equilibrium.png
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Summary
| ᏄᏍᏛ ᏗᎧᏃᏗ |
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] |
| ᎢᎦ | |
| ᏅᏓᏳᏓᎴᏅᎯ | Own work |
| ᏧᏬᏪᎳᏅᎯ | Thomas Shafee |
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- ↑ 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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| ᎢᎦ/ᎠᏟᎢᎵᏒ | ᎤᏍᏗ ᏓᏟᎶᏍᏛᎢ | Dimensions | ᎬᏗᏍᎩ | ᏍᏆᎳ ᎪᏪᎵ | |
|---|---|---|---|---|---|
| current | 23:23, 6 ᏚᏂᏅᏗ 2016 | | 3,000 × 1,902 (1.41 MB) | Cmdrjameson | Compressed with pngout. Reduced by 772kB (34% decrease). |
| 23:05, 19 ᎠᏄᏱ 2016 |  | 3,000 × 1,902 (2.16 MB) | Evolution and evolvability | Colour tweaks | |
| 12:05, 14 ᎥᏍᎩᎦ 2015 |  | 1,246 × 765 (476 KB) | Evolution and evolvability | Cross-wiki upload from en.wikipedia.org |
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