Literature DB >> 10089443

Decamers observed in the crystals of bovine pancreatic trypsin inhibitor.

J Lubkowski1, A Wlodawer.   

Abstract

The structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank.

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Year:  1999        PMID： 10089443     DOI： 10.1107/S0907444998011068

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN： 0907-4449


  5 in total

1.  Brownian dynamics simulation of protein solutions: structural and dynamical properties.

Authors:  Paolo Mereghetti; Razif R Gabdoulline; Rebecca C Wade
Journal:  Biophys J       Date:  2010-12-01       Impact factor: 4.033

2.  Protein self-association induced by macromolecular crowding: a quantitative analysis by magnetic relaxation dispersion.

Authors:  Karim Snoussi; Bertil Halle
Journal:  Biophys J       Date:  2005-01-21       Impact factor: 4.033

3.  Protein self-association in solution: the bovine pancreatic trypsin inhibitor decamer.

Authors:  Michael Gottschalk; Kandadai Venu; Bertil Halle
Journal:  Biophys J       Date:  2003-06       Impact factor: 4.033

4.  Structure of tick anticoagulant peptide at 1.6 A resolution complexed with bovine pancreatic trypsin inhibitor.

Authors:  R St Charles; K Padmanabhan; R V Arni; K P Padmanabhan; A Tulinsky
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

5.  BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path.

Authors:  Reem Mousa; Shifra Lansky; Gil Shoham; Norman Metanis
Journal:  Chem Sci       Date:  2018-05-02       Impact factor: 9.825
  5 in total

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