3V8O

Human Filamin C Ig - like Domains 4 and 5

3V8O の概要

• エントリーDOI: 10.2210/pdb3v8o/pdb
• 分子名称: Filamin-C, POTASSIUM ION (3 entities in total)
• 機能のキーワード: immunoglobulin like fold, muscle z disk, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14315
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41249.50

構造登録者

Sethi, R.,Ylanne, J. (登録日: 2011-12-23, 公開日: 2013-07-17, 最終更新日: 2023-09-13)

主引用文献

Sethi, R.,Seppala, J.,Tossavainen, H.,Ylilauri, M.,Ruskamo, S.,Pentikainen, O.T.,Pentikainen, U.,Permi, P.,Ylanne, J.
A novel structural unit in the N-terminal region of filamins.
J.Biol.Chem., 289:8588-8598, 2014

PubMed Abstract: Immunoglobulin-like (Ig) domains are a widely expanded superfamily that act as interaction motifs or as structural spacers in multidomain proteins. Vertebrate filamins (FLNs), which are multifunctional actin-binding proteins, consist of 24 Ig domains. We have recently discovered that in the C-terminal rod 2 region of FLN, Ig domains interact with each other forming functional domain pairs, where the interaction with signaling and transmembrane proteins is mechanically regulated by weak actomyosin contraction forces. Here, we investigated if there are similar inter-domain interactions around domain 4 in the N-terminal rod 1 region of FLN. Protein crystal structures revealed a new type of domain organization between domains 3, 4, and 5. In this module, domains 4 and 5 interact rather tightly, whereas domain 3 has a partially flexible interface with domain 4. NMR peptide titration experiments showed that within the three-domain module, domain 4 is capable for interaction with a peptide derived from platelet glycoprotein Ib. Crystal structures of FLN domains 4 and 5 in complex with the peptide revealed a typical β sheet augmentation interaction observed for many FLN ligands. Domain 5 was found to stabilize domain 4, and this could provide a mechanism for the regulation of domain 4 interactions.

PubMed: 24469451
DOI: 10.1074/jbc.M113.537456

実験手法

X-RAY DIFFRACTION (2.8 Å)