FEBS Letters | |
Mode of receptor binding and activation by plasminogen‐related growth factors | |
Miller, Maria2  Leonard, Edward J1  | |
[1] Laboratory of Immunobiology, NCI-Frederick Cancer Research and Development Center, Frederick, MD 21702, USA;Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, MD 21702-1201, USA | |
关键词: Hepatocyte growth factor; Macrophage stimulating protein; Plasminogen-related growth factor; Tumorigenesis; Receptor oligomerization; | |
DOI : 10.1016/S0014-5793(98)00533-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Hepatocyte growth factor/scatter factor (HGF/SF) and macrophage stimulating protein (MSP) are plasminogen-related kringle proteins that lost serine protease domain enzymatic activity and became ligands for cell surface tyrosine kinase receptors. They are activated by cleavage to disulfide-linked αβ chains. Surprisingly, despite structural similarities, the high affinity receptor binding regions of the two proteins are different: α chain for HGF, and β chain for MSP. We propose that after cleavage exposes a β chain binding site (high affinity for MSP, low affinity for HGF), monomeric ligand induces receptor dimerization and activation via α and β chain binding sites of different affinity.
【 授权许可】
Unknown
【 预 览 】
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