Specificity of Odor Recognition: The Three-Dimensional Structure of an Odorant Binding Protein

Abstract

This project uses single crystal x-ray diffraction methods for the detailed study of the interactions between effector molecules and their receptors. A small soluble protein from bovine nasal epithelium that binds a variety of odorants (OBP) will be the subject of this study. Crystals of OBP were obtained that contain 2 OBP dimers in the asymmetric unit. The structure is being solved using isomorphous heavy-atom derivatives and the maps will be enhanced by density averaging and map inversion. The polypeptide chain will be traced using the available OBP sequences (rat and bovine). The structures of several odorants bound to OBP will be determined by difference Fourier methods to understand the characteristics of the initial events in olfactory perception and the nature of chemical discrimination in smell. These studies will provide a unique insight for understanding the functioning of OBP and for answering important questions about receptor recognition in general.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1988
Accession Number
ADA197332

Entities

People

  • L. M. Amzel

Organizations

  • University of Texas at Dallas

Tags

Communities of Interest

  • C4I

DTIC Thesaurus Topics

  • Carrier Proteins
  • Crystals
  • Data Sets
  • Detectors
  • Diffraction
  • Discrimination
  • Electron Density
  • Electrons
  • Epithelium
  • Inversion
  • Molecules
  • Recognition
  • Single Crystals
  • Three Dimensional
  • Universities
  • X Rays
  • X-Ray Diffraction

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Quantum Chemistry
  • Vision Science/Vision Psychology/Cognitive Neuroscience.