1FZV
THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN AT 2.0A RESOLUTION
Summary for 1FZV
Entry DOI | 10.2210/pdb1fzv/pdb |
Related | 1FLT 2VPF |
Descriptor | PLACENTA GROWTH FACTOR, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total) |
Functional Keywords | cysteine-knot family, growth factor, angiogenesis, hormone-growth factor complex, hormone/growth factor |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P49763 |
Total number of polymer chains | 2 |
Total formula weight | 29980.48 |
Authors | Iyer, S.,Leonidas, D.D.,Swaminathan, G.J.,Maglione, D.,Battisti, M.,Tucci, M.,Persico, M.G.,Acharya, K.R. (deposition date: 2000-10-04, release date: 2001-05-09, Last modification date: 2024-10-16) |
Primary citation | Iyer, S.,Leonidas, D.D.,Swaminathan, G.J.,Maglione, D.,Battisti, M.,Tucci, M.,Persico, M.G.,Acharya, K.R. The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution. J.Biol.Chem., 276:12153-12161, 2001 Cited by PubMed Abstract: The angiogenic molecule placenta growth factor (PlGF) is a member of the cysteine-knot family of growth factors. In this study, a mature isoform of the human PlGF protein, PlGF-1, was crystallized as a homodimer in the crystallographic asymmetric unit, and its crystal structure was elucidated at 2.0 A resolution. The overall structure of PlGF-1 is similar to that of vascular endothelial growth factor (VEGF) with which it shares 42% amino acid sequence identity. Based on structural and biochemical data, we have mapped several important residues on the PlGF-1 molecule that are involved in recognition of the fms-like tyrosine kinase receptor (Flt-1, also known as VEGFR-1). We propose a model for the association of PlGF-1 and Flt-1 domain 2 with precise shape complementarity, consider the relevance of this assembly for PlGF-1 signal transduction, and provide a structural basis for altered specificity of this molecule. PubMed: 11069911DOI: 10.1074/jbc.M008055200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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