有哪些信誉好的足球投注网站a selection fit mechanism in bmp receptor ia as a possible source for bmp ligand-receptor promiscuity选择合适的机制在骨形态发生蛋白受体ia作为bmp可能源中的滥交.pdfVIP
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a selection fit mechanism in bmp receptor ia as a possible source for bmp ligand-receptor promiscuity选择合适的机制在骨形态发生蛋白受体ia作为bmp可能源中的滥交
A Selection Fit Mechanism in BMP Receptor IA as a Possible Source for BMP Ligand-Receptor Promiscuity 1 2 1 1 2 Stefan Harth , Alexander Kotzsch , Junli Hu , Walter Sebald , Thomas D. Mueller * ¨ ¨ ¨ ¨ ¨ ¨ 1 Lehrstuhl fur Physiologische Chemie II, Theodor-Boveri-Institut fur Biowissenschaften der Universitat Wurzburg, Wurzburg, Germany, 2 Lehrstuhl fur Molekulare ¨ ¨ ¨ Pflanzenphysiologie und Biophysik, Julius-von-Sachs Institut der Universitat Wurzburg, Wurzburg, Germany Abstract Background: Members of the TGF-b superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands. Structural and functional studies have been used to address the question of how specific signals can be deduced from a limited number of receptor combinations and to unravel the molecular mechanisms underlying the protein-protein recognition that allow such limited specificity. Principal Findings: In this study we have investigated how an antigen binding antibody fragment (Fab) raised against the extracellular domain of the BMP receptor type IA (BMPR-IA) recognizes the receptor’s BMP-2 binding epitope and thereby neutralizes BMP-2 receptor activation. The crystal structure of the complex of the BMPR-IA ectodomain bound to the Fab AbD1556 revealed that the contact surface of BMPR-IA overlaps
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