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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]
Ọjọ́ọdún
Orísun Iṣẹ́ onítọ̀hún
Olùdá Thomas Shafee

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Lábẹ́ àwọn àdéhùn wọ̀nyí:
  • ìdárúkọ – Ẹ gbọdọ̀ ṣe ọ̀wọ̀ tó yẹ, pèsè ìjápọ̀ sí ìwé-àṣe, kí ẹ sì sọ bóyá ìyípadà wáyé. Ẹ le ṣe èyí lórísi ọ̀nà tó bojúmu, sùgbọ́n tí kò ní dà bii pé oníìwé-àṣe fọwọ́ sí yín tàbí lílò yín.
  1. 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.
  2. (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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lọ́wọ́23:23, 6 Oṣù Ọ̀wàrà 2016Àwòrán kékeré fún ní 23:23, 6 Oṣù Ọ̀wàrà 20163,000 × 1,902 (1.41 MB)CmdrjamesonCompressed with pngout. Reduced by 772kB (34% decrease).
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