1fzv
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(New page: 200px<br /> <applet load="1fzv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzv, resolution 2.00Å" /> '''THE CRYSTAL STRUCTU...)
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Revision as of 14:52, 12 November 2007
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THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN AT 2.0A RESOLUTION
Overview
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.
About this Structure
1FZV is a Single protein structure of sequence from Homo sapiens with MPD as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution., Iyer S, Leonidas DD, Swaminathan GJ, Maglione D, Battisti M, Tucci M, Persico MG, Acharya KR, J Biol Chem. 2001 Apr 13;276(15):12153-61. Epub 2000 Nov 7. PMID:11069911
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