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PDBsum entry 2xac
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Transferase/signaling protein
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PDB id
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2xac
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References listed in PDB file
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Key reference
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Title
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Structural insights into the binding of vascular endothelial growth factor-B by vegfr-1(d2): recognition and specificity.
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Authors
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S.Iyer,
P.I.Darley,
K.R.Acharya.
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Ref.
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J Biol Chem, 2010,
285,
23779-23789.
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PubMed id
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Abstract
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The formation of blood vessels (angiogenesis) is a highly orchestrated sequence
of events involving crucial receptor-ligand interactions. Angiogenesis is
critical for physiological processes such as development, wound healing,
reproduction, tissue regeneration and remodeling. It also plays a major role in
sustaining tumor progression and chronic inflammation. Vascular Endothelial
Growth Factor-B (VEGF-B), a member of the VEGF family of angiogenic growth
factors, effects blood vessel formation by binding to a tyrosine kinase
receptor, VEGFR-1. There is growing evidence of the important role played by
VEGF-B in physiological and pathological vasculogenesis. Development of VEGF-B
antagonists, which inhibit the interaction of this molecule with its cognate
receptor, would be important for the treatment of pathologies associated
specifically with this growth factor. In this study we present the crystal
structure of the complex of VEGF-B with domain 2 of VEGFR-1 at 2.7A resolution.
Our analysis reveals that each molecule of the ligand engages two receptor
molecules using two symmetrical binding sites. Based on these interactions we
identify the receptor-binding determinants on VEGF-B and shed light on the
differences in specificity towards VEGFR-1 among the different VEGF homologs.
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