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Evolution of shape complementarity and catalytic efficiency from a primordial antibody template

Academic Article
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Overview

authors

  • Xu, J. A.
  • Deng, Q. L.
  • Chen, J. G.
  • Houk, K. N.
  • Bartek, J.
  • Hilvert, Donald M.
  • Wilson, Ian

publication date

  • December 1999

journal

  • Science  Journal

abstract

  • The crystal structure of an efficient Diels-Alder antibody catalyst at 1.9 angstrom resolution reveals almost perfect shape complementarity with its transition state analog. Comparison with highly related progesterone and Diels-Alderase antibodies that arose from the same primordial germ line template shows the relatively subtle mutational steps that were able to evolve both structural complementarity and catalytic efficiency.

subject areas

  • Antibodies, Catalytic
  • Binding Sites, Antibody
  • Catalysis
  • Chemistry, Physical
  • Crystallography, X-Ray
  • Evolution, Molecular
  • Haptens
  • Hydrogen Bonding
  • Immunoglobulin Fab Fragments
  • Ligands
  • Models, Molecular
  • Mutation
  • Physicochemical Phenomena
  • Progesterone
  • Protein Conformation
  • Solubility
  • Temperature
  • Templates, Genetic
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.286.5448.2345

PubMed ID

  • 10600746
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Additional Document Info

start page

  • 2345

end page

  • 2348

volume

  • 286

issue

  • 5448

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