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Conformational flexibility in crystal structures of human 11 β-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation

Academic Article
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Overview

authors

  • Hosfield, David J
  • Wu, Y.
  • Skene, R. J.
  • Hilgers, M.
  • Jennings, A.
  • Snell, G. P.
  • Aertgeerts, K.

publication date

  • 2005

journal

  • Journal of Biological Chemistry  Journal

subject areas

  • 11-beta-Hydroxysteroid Dehydrogenases
  • Amino Acid Motifs
  • Binding Sites
  • Cloning, Molecular
  • Cortisone
  • Crystallography, X-Ray
  • Cysteine
  • Diabetes Mellitus, Type 2
  • Dimerization
  • Disulfides
  • Endoplasmic Reticulum
  • Enzyme Inhibitors
  • Escherichia coli
  • Glucocorticoids
  • Humans
  • Hydrocortisone
  • Kinetics
  • Mass Spectrometry
  • Models, Molecular
  • Mutagenesis
  • Obesity
  • Oxygen
  • Point Mutation
  • Proline
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M411104200

PubMed ID

  • 15513927
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Additional Document Info

start page

  • 4639

end page

  • 4648

volume

  • 280

issue

  • 6

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