
Domain communication in the dynamical structure of human immunodeficiency virus 1 protease.
Author(s) -
William E. Harte,
S. Swaminathan,
Muzammil M. Mansuri,
Jörg Martin,
Ivan Rosenberg,
David L. Beveridge
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.22.8864
Subject(s) - protease , domain (mathematical analysis) , dimer , molecular dynamics , human immunodeficiency virus (hiv) , protein domain , protein structure , biological system , function (biology) , hiv 1 protease , virus , aqueous solution , enzyme , computational biology , chemistry , biology , biophysics , virology , mathematics , genetics , computational chemistry , biochemistry , gene , mathematical analysis , organic chemistry
A dynamical model for the structure of the human immunodeficiency virus 1 (HIV-1) protease dimer in aqueous solution has been developed on the basis of molecular dynamics simulation. The model provides an accurate account of the crystal geometry and also a prediction of the structural reorganization expected to occur in the protein in aqueous solution compared to the crystalline environment. Analysis of the results by means of dynamical cross-correlation coefficients for atomic displacements indicates that domain-domain communication is present in the protein in the form of a molecular "cantilever" and is likely to be involved in enzyme function at the molecular level. The dynamical structure also suggests information that may ultimately be useful in understanding and further development of specific inhibitors of HIV-1 protease.