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Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study.
Department of Biochemistry, University of Oxford, U.K.
The solution structure of human insulin-like growth factor 1 has been investigated with a combination of nuclear magnetic resonance and restrained molecular dynamics methods. The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins.
PMID: 2036417 [PubMed - indexed for MEDLINE]
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Cited by 4 PubMed Central articles
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The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5.
Zesławski W, Beisel HG, Kamionka M, Kalus W, Engh RA, Huber R, Lang K, Holak TA.
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[EMBO J. 2001]
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Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions.
Kalus W, Zweckstetter M, Renner C, Sanchez Y, Georgescu J, Grol M, Demuth D, Schumacher R, Dony C, Lang K, et al.
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[EMBO J. 1998]
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Mutations in the B-domain of insulin-like growth factor-I influence the oxidative folding to yield products with modified biological properties.
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[Biochem J. 1995]
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Structures reported by this article