5CTI

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 of type I collagen (native form)

5CTI の概要

• エントリーDOI: 10.2210/pdb5cti/pdb
• 分子名称: Collagen alpha-1(I) chain,Collagen alpha-1(IX) chain, Collagen alpha-2(I) chain,Collagen alpha-2(IX) chain, Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain, ... (5 entities in total)
• 機能のキーワード: collagen, hetero-trimerization, chain stagger, chain register, triple helix, structural protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : P20849 Q14055 Q14050
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 21191.97

構造登録者

Boudko, S.P.,Bachinger, H.P. (登録日: 2015-07-24, 公開日: 2016-08-03, 最終更新日: 2023-09-27)

主引用文献

Boudko, S.P.,Bachinger, H.P.
Structural insight for chain selection and stagger control in collagen.
Sci Rep, 6:37831-37831, 2016

PubMed Abstract: Collagen plays a fundamental role in all known metazoans. In collagens three polypeptides form a unique triple-helical structure with a one-residue stagger to fit every third glycine residue in the inner core without disturbing the poly-proline type II helical conformation of each chain. There are homo- and hetero-trimeric types of collagen consisting of one, two or three distinct chains. Thus there must be mechanisms that control composition and stagger during collagen folding. Here, we uncover the structural basis for both chain selection and stagger formation of a collagen molecule. Three distinct chains (α1, α2 and α3) of the non-collagenous domain 2 (NC2) of type IX collagen are assembled to guide triple-helical sequences in the leading, middle and trailing positions. This unique domain opens the door for generating any fragment of collagen in its native composition and stagger.

PubMed: 27897211
DOI: 10.1038/srep37831

実験手法

X-RAY DIFFRACTION (1.8994 Å)