English  |  正體中文  |  简体中文  |  Items with full text/Total items : 54367/62174 (87%)
Visitors : 14664033      Online Users : 94
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTHU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    National Tsing Hua University Institutional Repository > 理學院 > 化學系 > 期刊論文 >  Solution structure of the ligand binding domain of the fibroblast growth factor receptor: Role of heparin in the activation of the receptor

    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56540

    Title: Solution structure of the ligand binding domain of the fibroblast growth factor receptor: Role of heparin in the activation of the receptor
    Authors: Hung KW;Kurnar TKS;Kathir KM;Xu P;Ni F;Ji HH;Chen MC;Yang CC;Lin FP;Chiu IM;Yu C
    教師: 余靖
    Date: 2005
    Publisher: American Chemical Society
    Relation: Biochemistry -Pennsylvania then Washington,American Chemical Society,Volume: 44,Issue: 48,Pages: 15787-15798 Published: DEC 6 2005
    Abstract: The three-dimensional solution Structure of the ligand binding D2 domain of the fibroblast growth factor receptor (FGFR) is determined using Multidimensional NMR techniques. The atomic root mean-square distribution for the backbone atoms in the structured region is 0.64 angstrom. Secondary structural elements in the D2 domain include beta-strands arranged antiparallely into two layers of beta-sheets. The Structure of the D2 domain is characterized by the presence of a short flexible helix that protrudes Out Of the layers of beta-sheets. Results of size exclusion chromatography and sedimentation velocity experiments show that the D2 domain exists in a monomeric state both in the presence and in the absence of bound,sucrose octasulfate (SOS), a Structural analogue of heparin. Comparison of the Solution structure of the D2 domain with the crystal structure of the protein (D2 domain) in the FGF signaling complex reveals significant differences, suggesting that ligand (FGF) binding may induce significant conformational changes in the receptor. SOS binding sites in the D2 domain have been mapped on the basis of the H-1-N-15 chemical shift perturbation data. SOS binds to the positively charged residues located in beta-strand III and the flexible helix. isothermal titration calorimetry data indicate that the ligand (hFGF-1) binds strongly (K-d similar to 10(-9) M) to the D2 domain even in the absence of SOS. Binding of SOS to either the D2 domain or hFGF-1 does not seem to be the driving force for the formation of the D2-hFGF-1 binary complex. The function of SOS binding appears to stabilize the preformed D2-FGF binary complex.
    URI: http://pubs.acs.org/
    Appears in Collections:[化學系] 期刊論文

    Files in This Item:

    File Description SizeFormat


    SFX Query


    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback