ܠܦܦܐ:Serpin mechanism.png
ܥܓܪܐ ܕܓܠܚܐ: 725 × 599 ܦܩܣܠ. Other resolutions: 290 × 240 ܦܩܣܠ | 581 × 480 ܦܩܣܠ | 929 × 768 ܦܩܣܠ | 1,239 × 1,024 ܦܩܣܠ | 1,800 × 1,488 ܦܩܣܠ.
ܠܦܦܐ ܫܪܫܝܐ (1,800 × 1,488 ܦܩܣܠ، ܥܓܪܐ ܕܠܦܦܐ: 513 KB، ܐܕܫܐ ܕ MIME: image/png)
ܦܣܝܩܬ̈ܐ
| Description |
English: Serine proteases operate by a two-step catalytic mechanism. First, the substrate (blue) is attacked by the catalytic triad (red) to form an acyl-enzyme intermediate. The intermediate is typically resolved by hydrolysis by water. However, when the reactive centre loop (RCL) of a serpin is attacked, the conformational change (blue arrow) pulls the catalytic triad out of position, preventing it from completing catalysis. (Based on PDB: 1K9O, 1EZX) |
| ܣܝܩܘܡܐ | |
| ܡܒܘܥܐ | Own work |
| ܣܝܘܡܐ | Thomas Shafee |
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| ܗܫܝܐ | 09:56, 22 ܒܟܢܘܢ ܩܕܡ 2015 | | 1,800 × 1,488 (513 KB) | Evolution and evolvability | Higher resolution |
| 05:19, 19 ܒܟܢܘܢ ܩܕܡ 2015 |  | 1,362 × 1,126 (300 KB) | Evolution and evolvability | Minor arrow correction | |
| 05:08, 19 ܒܟܢܘܢ ܩܕܡ 2015 |  | 1,362 × 1,126 (300 KB) | Evolution and evolvability | added arrow and removed transparency | |
| 05:04, 19 ܒܟܢܘܢ ܩܕܡ 2015 |  | 1,362 × 1,114 (360 KB) | Evolution and evolvability | Cross-wiki upload from en.wikipedia.org |
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