4
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Protein conformer selection by ligand binding observed with crystallography.

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          A large-scale movement between "closed" and "open" conformations of a protein loop was observed directly with protein crystallography by trapping individual conformers through binding of an exogenous ligand and characterization with solution kinetics. The buried indole ring of Trp191 in cytochrome c peroxidase (CCP) was displaced by exogenous ligands, causing a conformational change of loop Pro190-Asn195 and exposing Trp191 to the protein surface. Kinetic measurements are consistent with a two-step binding mechanism in which the rate-limiting step is a transition of the protein to the open state, which then binds the ligand. This large-scale conformational change of a functionally important region of CCP is independent of ligand and indicates that about 4% of the wild-type protein is in the open form in solution at any given time.

          Related collections

          Author and article information

          Journal
          Protein Sci.
          Protein science : a publication of the Protein Society
          Wiley
          0961-8368
          0961-8368
          Jan 1998
          : 7
          : 1
          Affiliations
          [1 ] Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
          Article
          10.1002/pro.5560070107
          2143825
          9514261
          052f5dd5-089b-4405-852b-dcc833f9e0c8
          History

          Comments

          Comment on this article