翻訳と辞書 |
Beta-sandwich : ウィキペディア英語版 | Beta-sandwich
β-sandwich domains are characterized by two opposing antiparallel β-sheets. The number of strands found in the sandwich motif may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of ''Staphylococcus aureus'' Adhesin and in modules that bind fibronectin as found in Tenascin (Third Fibronectin Type III Repeat). The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 β-strands. ==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Beta-sandwich」の詳細全文を読む
スポンサード リンク
翻訳と辞書 : 翻訳のためのインターネットリソース |
Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.
|
|