1rv6: Difference between revisions
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{{STRUCTURE_1rv6| PDB=1rv6 | SCENE= }} | {{STRUCTURE_1rv6| PDB=1rv6 | SCENE= }} | ||
===Crystal Structure of PlGF in Complex with Domain 2 of VEGFR1=== | |||
{{ABSTRACT_PUBMED_14684734}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/VGFR1_HUMAN VGFR1_HUMAN]] Note=Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages. Note=Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia. | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PLGF_HUMAN PLGF_HUMAN]] Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth.<ref>PMID:21215706</ref> [[http://www.uniprot.org/uniprot/VGFR1_HUMAN VGFR1_HUMAN]] Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.<ref>PMID:8248162</ref><ref>PMID:18593464</ref><ref>PMID:18515749</ref><ref>PMID:20512933</ref><ref>PMID:7824266</ref><ref>PMID:8605350</ref><ref>PMID:9299537</ref><ref>PMID:11141500</ref><ref>PMID:11811792</ref><ref>PMID:11312102</ref><ref>PMID:14633857</ref><ref>PMID:12796773</ref><ref>PMID:15735759</ref><ref>PMID:16685275</ref><ref>PMID:18079407</ref><ref>PMID:18583712</ref><ref>PMID:20551949</ref><ref>PMID:21752276</ref> | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:014684734</ref><references group="xtra"/> | <ref group="xtra">PMID:014684734</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Christinger, H W.]] | [[Category: Christinger, H W.]] | ||