The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 Å resolution
The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 Å resolution
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DOI：
10.1074/jbc.m008055200
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发表时间：
2001-04-13
影响因子：
4.8
通讯作者：
Acharya, KR
中科院分区：
文献类型：
--
作者：
Iyer, S;Leonidas, DD;Acharya, KR
血管生成分子胎盘生长因子（PlGF）是半胱氨酸结生长因子家族的成员。在这项研究中，人PlGF蛋白的成熟同种型PlGF-1在晶体学不对称单元中结晶为同源二聚体，并在2.0埃分辨率下阐明其晶体结构。PlGF-1的整体结构与血管内皮生长因子（VEGF）的结构相似，其与血管内皮生长因子（VEGF）共享42%氨基酸序列同一性。基于结构和生物化学数据，我们绘制了PlGF-1分子上参与fms样酪氨酸激酶受体（Flt-1，也称为VEGFR-1）识别的几个重要残基。我们提出了一个模型，为协会的PlGF-1和Flt-1结构域2与精确的形状互补性，考虑的相关性PlGF-1的信号转导，这种大会，并提供了一个结构的基础上改变特异性的这种分子。
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 Angstrom 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.