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Crystal structure of a cell surface receptor（uPAR） in its ligand-free conformation reveals the exposure of an unusually large hydrophobic area

Crystal structure of a cell surface receptor（uPAR） in its ...

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第四届中国结构生物学学术讨论会

作者： Baoyu Zhao Cai Yuan Rui Li Michael Ploug nicolai sidenius Mingdong Huang Fujian Institute of Research on the Structure of Matter The Chinese Academy of Sciences Finsen Laboratory Rigshospitalet & Biotech Research and Innovation Centre (BRIC) Copenhagen Biocenter Ole Maal?es Vej 5 DK-2200 Copenhagen N Denmark San Raffaele Scientific Institute

Proteins typically fold in a way to have their hydrophobic residues buried in the core of proteins while the hydrophilic residues exposed on protein surface. The exposure of large hydrophobic patch to solvent is thermodynamically unfavorable, and is not commonly observed. Cell surface receptor urokinase-type plasminogen activator receptor（uPAR） has a large hydrophobic patch in its central ligand binding pocket. Upon the ligand（uPA） binding, this hydrophobic patch on uPAR is sequestered, forming a highly stable and tight-binding complex（Qing Huai, 2006）. The crystallization of uPAR ectodomains in its ligand-free conformation is expected to be difficult, but has been a long sought goal. With the help of an anti-uPAR antibody（8B12）, we recently succeed to crystallize the uPAR:8B12 complex in the absence of any ligands, and determined the crystal structure of uPAR in the ligand-free conformation. Surprisingly, uPAR adopts a conformation similar to its ligand-bound state, exposing a large hydrophobic area to solvent. This observation is different from the previous speculation and biochemical studies（Cai Yuan, 2007 and Haydyn D. T. Mertens, 2012）. uPAR is a glycolipid-anchored cell surface receptor and consists of three Ly6/uPAR/α-neurotoxin-like（LU） domains. Extensive degree of inter-domain flexibility was expected and was indeed observed in solution by biochemical studies including small angle X-ray scattering. However, Our recent uPAR:8B12 structure showed no inter-domain flexibility and the conformation of unliganded uPAR is identical to the ligand-bound conformation. Further functional studies are underway to examine the functional consequences of these structural observations.

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