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Volumn 127, Issue 16, 2005, Pages 5778-5779

Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the 1C4 and 2So conformations of a bioactive heparin-like hexasaccharide

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR 1; HEPARIN; POLYSACCHARIDE; SYNTHETIC GLYCOSAMINOGLYCAN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 20244368809     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja043363y     Document Type: Article
Times cited : (67)

References (27)
  • 17
    • 1542328863 scopus 로고    scopus 로고
    • For a recent revision of applications in the carbohydrate field, see: Johnson, M. A.; Pinto, B. M. Carbohydr. Res. 2004, 339, 907-928.
    • (2004) Carbohydr. Res. , vol.339 , pp. 907-928
    • Johnson, M.A.1    Pinto, B.M.2
  • 20
    • 17744388084 scopus 로고    scopus 로고
    • note
    • c for free FGF-1 was 10.4 ns. Thus, the protein is a monomer in the complex. HSQC-based chemical shift perturbation analysis of FGF-1 upon binding of 1, with 3D-HNCO, HNCA, HNCOCA, TOCSY-HSQC, NOESY, TOCSY, and NOESY-HSQC experiments at 800 MHz allowed the deduction of the 3D structure of the complex. This will be published elsewhere.
  • 22
    • 17744374456 scopus 로고    scopus 로고
    • note
    • 2O, pH 6.0), and a 1.1:1 excess of 1. Cross relaxation rates were obtained from the build up curves of NOEs versus mixing time. Build up curves showed good linearity for these mixing times.
  • 25
    • 17744365920 scopus 로고    scopus 로고
    • note
    • o conformations is given in the Supporting Information.
  • 26
    • 17744390330 scopus 로고    scopus 로고
    • note
    • The filtered NOESY also permitted us to distinguish intermolecular NOEs between 1 and the chains of Lys127, Arg133, and Lys142, thus providing a 3D view of the orientation of 1 within the binding site (see ref 16).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.