2AAV

Solution NMR structure of Filamin A domain 17

2AAV の概要

• エントリーDOI: 10.2210/pdb2aav/pdb
• 関連するPDBエントリー: 2BP3
• NMR情報: BMRB: 6730
• 分子名称: Filamin A (1 entity in total)
• 機能のキーワード: filamin a domain 17, beta-sandwich, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cell cortex: P21333
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10075.15

構造登録者

Nakamura, F.,Pudas, R.,Heikkinen, O.,Permi, P.,Kilpelainen, I.,Munday, A.D.,Hartwig, J.H.,Stossel, T.P.,Ylanne, J. (登録日: 2005-07-14, 公開日: 2006-05-02, 最終更新日: 2024-05-29)

主引用文献

Nakamura, F.,Pudas, R.,Heikkinen, O.,Permi, P.,Kilpelainen, I.,Munday, A.D.,Hartwig, J.H.,Stossel, T.P.,Ylanne, J.
The structure of the GPIb-filamin A complex
Blood, 107:1925-1932, 2006

PubMed Abstract: Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with numerous intracellular binding partners, anchors the platelet adhesion glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the GPIbalpha binding site to a single domain of FLNa and resolved the structure of this domain and its interaction complex with the corresponding GPIbalpha cytoplasmic domain. This is the first atomic structure of this class of membrane glycoprotein-cytoskeleton connection. GPIbalpha binds in a groove formed between the C and D beta strands of FLNa domain 17. The interaction is strikingly similar to that between the beta7 integrin tail and a different FLNa domain, potentially defining a conserved motif for FLNa binding. Nevertheless, the structures also reveal specificity of the interfaces, which explains different regulatory mechanisms. To verify the topology of GPIb-FLNa interaction we also purified the native complex from platelets and showed that GPIb interacts with the C-terminus of FLNa, which is in accordance with our biochemical and structural data.

PubMed: 16293600
DOI: 10.1182/blood-2005-10-3964

実験手法

SOLUTION NMR