2KI6

The FGF1-S100A13-C2A hetero-hexameric complex structure: A component in the non-classical pathway for FGF1 secretion

2KI6 の概要

• エントリーDOI: 10.2210/pdb2ki6/pdb
• 分子名称: Synaptotagmin-1, Heparin-binding growth factor 1, Protein S100-A13, ... (4 entities in total)
• 機能のキーワード: fgf1-s100a13-c2a hetero-hexameric complex, fgf1, s100a13, c2a, calcium, cell junction, cytoplasmic vesicle, glycoprotein, lipoprotein, membrane, metal-binding, palmitate, phosphoprotein, synapse, transmembrane, acetylation, alternative splicing, angiogenesis, developmental protein, differentiation, growth factor, heparin-binding, mitogen, polymorphism, protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein: P21579; Secreted: P05230; Cytoplasm: Q99584 Q99584
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 82781.22

構造登録者

Krishna, S.M.,Rani, S.G.,Yu, C. (登録日: 2009-04-28, 公開日: 2010-03-09, 最終更新日: 2024-11-20)

主引用文献

Mohan, S.K.,Rani, S.G.,Yu, C.
The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion.
J.Biol.Chem., 285:15464-15475, 2010

PubMed Abstract: Fibroblast growth factors (FGFs) are key regulators of cell proliferation, tumor-induced angiogenesis, and migration. FGFs are essential for early embryonic development, organ formation, and angiogenesis. FGF1 also plays an important role in inflammation, wound healing, and restenosis. The biological effects of FGF1 are mediated through the activation of the four transmembrane phosphotyrosine kinase fibroblast growth factor receptors in the presence of heparin sulfate proteoglycans and, therefore, require the release of the protein into the extracellular space. FGF1 is exported through a non-classical release pathway involving the formation of a specific multiprotein complex. The protein constituents of this complex include FGF1, S100A13, and the p40 form of synaptotagmin 1 (Syt1). Because FGF1 plays an important role in tumor formation, it is clear that preventing the formation of the multiprotein complex would be an effective strategy to inhibit a wide range of cancers. To understand the molecular events in the FGF1 release pathway, we studied the FGF1-S100A13 tetrameric and FGF1-S100A13-C2A hexameric complex structures, which are both complexes possibly formed during the non-classical pathway of FGF1 release.

PubMed: 20220137
DOI: 10.1074/jbc.M109.066357

実験手法

SOLUTION NMR