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Alanine Scanning Mutagenesis of a Type 1 Insulin-like Growth Factor Receptor Ligand Binding Site

Alanine Scanning Mutagenesis of a Type 1 Insulin-like Growth Factor Receptor Ligand Binding Site THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 276, No. 47, Issue of November 23, pp. 43980 –43986, 2001 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Alanine Scanning Mutagenesis of a Type 1 Insulin-like Growth Factor Receptor Ligand Binding Site* Received for publication, April 2, 2001, and in revised form, July 3, 2001 Published, JBC Papers in Press, August 10, 2001, DOI 10.1074/jbc.M102863200 Jonathan Whittaker‡§, Andreas V. Groth‡, Dennis C. Mynarcik¶, Lene Pluzek‡, Vibeke L. Gadsbøll‡, and Linda J. Whittaker‡ From the ‡Receptor Biology Laboratory, Hagedorn Research Institute, Gentofte 2820, Denmark and ¶the Department of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794 The high resolution crystal structure of an N-terminal for IGF-I in transgenic mice results in both embryonic and fragment of the IGF-I receptor, has been reported. While post-natal growth retardation (2). In contrast, the effects of this fragment is itself devoid of ligand binding activity, disruption of the IGF-II gene are confined to growth retarda- mutational analysis has indicated that its N terminus tion during the embryonic period (2). In addition to being (L1, amino acids 1–150) and the C terminus of its cys- http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Biological Chemistry Unpaywall

Alanine Scanning Mutagenesis of a Type 1 Insulin-like Growth Factor Receptor Ligand Binding Site

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0021-9258
DOI
10.1074/jbc.m102863200
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Abstract

THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 276, No. 47, Issue of November 23, pp. 43980 –43986, 2001 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Alanine Scanning Mutagenesis of a Type 1 Insulin-like Growth Factor Receptor Ligand Binding Site* Received for publication, April 2, 2001, and in revised form, July 3, 2001 Published, JBC Papers in Press, August 10, 2001, DOI 10.1074/jbc.M102863200 Jonathan Whittaker‡§, Andreas V. Groth‡, Dennis C. Mynarcik¶, Lene Pluzek‡, Vibeke L. Gadsbøll‡, and Linda J. Whittaker‡ From the ‡Receptor Biology Laboratory, Hagedorn Research Institute, Gentofte 2820, Denmark and ¶the Department of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794 The high resolution crystal structure of an N-terminal for IGF-I in transgenic mice results in both embryonic and fragment of the IGF-I receptor, has been reported. While post-natal growth retardation (2). In contrast, the effects of this fragment is itself devoid of ligand binding activity, disruption of the IGF-II gene are confined to growth retarda- mutational analysis has indicated that its N terminus tion during the embryonic period (2). In addition to being (L1, amino acids 1–150) and the C terminus of its cys-

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Journal of Biological Chemistry – Unpaywall

Published: Nov 1, 2001

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