2M74

1H, 13C and 15N assignments of the four N-terminal domains of human fibrillin-1

2M74 の概要

• エントリーDOI: 10.2210/pdb2m74/pdb
• NMR情報: BMRB: 18843
• 分子名称: Fibrillin-1 (1 entity in total)
• 機能のキーワード: structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P35555
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14120.08

構造登録者

Yadin, D.A.,Robertson, I.B.,Jensen, S.A.,Handford, P.A.,Redfield, C. (登録日: 2013-04-17, 公開日: 2013-09-25, 最終更新日: 2024-10-30)

主引用文献

Yadin, D.A.,Robertson, I.B.,McNaught-Davis, J.,Evans, P.,Stoddart, D.,Handford, P.A.,Jensen, S.A.,Redfield, C.
Structure of the Fibrillin-1 N-Terminal Domains Suggests that Heparan Sulfate Regulates the Early Stages of Microfibril Assembly.
Structure, 21:1743-1756, 2013

PubMed Abstract: The human extracellular matrix glycoprotein fibrillin-1 is the primary component of the 10- to 12-nm-diameter microfibrils, which perform key structural and regulatory roles in connective tissues. Relatively little is known about the molecular mechanisms of fibrillin assembly into microfibrils. Studies using recombinant fibrillin fragments indicate that an interaction between the N- and C-terminal regions drives head-to-tail assembly. Here, we present the structure of a fibrillin N-terminal fragment comprising the fibrillin unique N-terminal (FUN) and the first three epidermal growth factor (EGF)-like domains (FUN-EGF3). Two rod-like domain pairs are separated by a short, flexible linker between the EGF1 and EGF2 domains. We also show that the binding site for the C-terminal region spans multiple domains and overlaps with a heparin interaction site. These data suggest that heparan sulfate may sequester fibrillin at the cell surface via FUN-EGF3 prior to aggregation of the C terminus, thereby regulating microfibril assembly.

PubMed: 24035709
DOI: 10.1016/j.str.2013.08.004

実験手法

SOLUTION NMR