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PDBsum entry 2ki6

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Protein transport PDB id
2ki6
Contents
Protein chains
128 a.a.
133 a.a.
98 a.a.

References listed in PDB file
Key reference
Title The heterohexameric complex structure, A component in the non-Classical pathway for fibroblast growth factor 1 (fgf1) secretion.
Authors S.K.Mohan, S.G.Rani, C.Yu.
Ref. J Biol Chem, 2010, 285, 15464-15475.
PubMed id 20220137
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.
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