Structural Basis for Specific Recognition of Reelin by Its Receptors
作者： Norihisa Yasui , Terukazu Nogi , Junichi Takagi
DOI: 10.1016/J.STR.2010.01.010
关键词:
摘要: Summary Apolipoprotein E receptor 2 (ApoER2) and very-low-density lipoprotein receptor, members of the low-density (LDLR) protein family, function as neuronal receptors for a secreted glycoprotein reelin during brain development. In both receptors, first LDLR class A (LA1) module is sufficient to bind reelin. Analysis 2.6 crystal structure receptor-binding fragment in complex with LA1 ApoER2 revealed that Lys2467 recognized by conserved Trp residue calcium-coordinating acidic residues from LA1, which together Lys2360 plays critical role interaction. This "double-Lys" recognition mode is, fact, shared among other family proteins ligand binding. The interface between covers small surface area ∼350 on each side, ensures stable formation under physiological conditions. An examination structure-guided mutagenesis on interface key features this
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G. Bu, H.J. Geuze, G.J. Strous, A.L. Schwartz, 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. The EMBO Journal. ,vol. 14, pp. 2269- 2280 ,(1995) , 10.1002/J.1460-2075.1995.TB07221.X
Zbyszek Otwinowski, Wladek Minor, Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology. ,vol. 276, pp. 307- 326 ,(1997) , 10.1016/S0076-6879(97)76066-X
Dong-Ho Kim, Hiroaki Iijima, Kaoru Goto, Juro Sakai, Hirofumi Ishii, Hyoun-Ju Kim, Hiroyuki Suzuki, Hisatake Kondo, Shigeru Saeki, Tokuo Yamamoto, Human Apolipoprotein E Receptor 2 A NOVEL LIPOPROTEIN RECEPTOR OF THE LOW DENSITY LIPOPROTEIN RECEPTOR FAMILY PREDOMINANTLY EXPRESSED IN BRAIN Journal of Biological Chemistry. ,vol. 271, pp. 8373- 8380 ,(1996) , 10.1074/JBC.271.14.8373
J. Sakai, A. Hoshino, S. Takahashi, Y. Miura, H. Ishii, H. Suzuki, Y. Kawarabayasi, T. Yamamoto, Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene. Journal of Biological Chemistry. ,vol. 269, pp. 2173- 2182 ,(1994) , 10.1016/S0021-9258(17)42151-X
Brian W. Howell, Richard Hawkes, Philippe Soriano, Jonathan A. Cooper, Neuronal position in the developing brain is regulated by mouse disabled-1 Nature. ,vol. 389, pp. 733- 737 ,(1997) , 10.1038/39607
Christian Brandes, Larissa Kahr, Walter Stockinger, Thomas Hiesberger, Wolfgang J. Schneider, Johannes Nimpf, Alternative Splicing in the Ligand Binding Domain of Mouse ApoE Receptor-2 Produces Receptor Variants Binding Reelin but Not α2-Macroglobulin Journal of Biological Chemistry. ,vol. 276, pp. 22160- 22169 ,(2001) , 10.1074/JBC.M102662200
Shiori Kohno, Takao Kohno, Yoshimi Nakano, Kenta Suzuki, Moe Ishii, Hideaki Tagami, Atsushi Baba, Mitsuharu Hattori, Mechanism and significance of specific proteolytic cleavage of Reelin Biochemical and Biophysical Research Communications. ,vol. 380, pp. 93- 97 ,(2009) , 10.1016/J.BBRC.2009.01.039
Y. Jossin, L. Gui, A. M. Goffinet, Processing of Reelin by Embryonic Neurons Is Important for Function in Tissue But Not in Dissociated Cultured Neurons The Journal of Neuroscience. ,vol. 27, pp. 4243- 4252 ,(2007) , 10.1523/JNEUROSCI.0023-07.2007
Gabriella D'Arcangelo, Graham G. Miao, Shu-Cheng Chen, Holly D. Scares, James I. Morgan, Tom Curran, A protein related to extracellular matrix proteins deleted in the mouse mutant reeler Nature. ,vol. 374, pp. 719- 723 ,(1995) , 10.1038/374719A0
Donghan Lee, Joseph D. Walsh, Irina Mikhailenko, Ping Yu, Molly Migliorini, Yibing Wu, Susan Krueger, Joseph E. Curtis, Bradley Harris, Stephen Lockett, Steve C. Blacklow, Dudley K. Strickland, Yun-Xing Wang, RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Molecular Cell. ,vol. 22, pp. 423- 430 ,(2006) , 10.1016/J.MOLCEL.2006.04.011