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PDBsum entry 2ki6
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Protein transport
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PDB id
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2ki6
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Contents |
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128 a.a.
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133 a.a.
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98 a.a.
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References listed in PDB file
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Key reference
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Title
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The heterohexameric complex structure, A component in the non-Classical pathway for fibroblast growth factor 1 (fgf1) secretion.
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Authors
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S.K.Mohan,
S.G.Rani,
C.Yu.
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Ref.
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J Biol Chem, 2010,
285,
15464-15475.
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PubMed id
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Abstract
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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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