Portal de Periódicos da CAPES

Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers

1997; Wiley; Volume: 28; Issue: 4 Linguagem: Inglês

10.1002/(sici)1097-0134(199708)28

1097-0134

Swagata Dasgupta, Ganesh Iyer, Stephen H. Bryant, Charles E. Lawrence, Jeffrey A. Bell,

Protein Structure and Dynamics

Proteins: Structure, Function, and BioinformaticsVolume 28, Issue 4 p. 494-514 Research Article Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers Swagata Dasgupta, Swagata Dasgupta Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Search for more papers by this authorGanesh H. Iyer, Ganesh H. Iyer Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Search for more papers by this authorStephen H. Bryant, Stephen H. Bryant National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894Search for more papers by this authorCharles E. Lawrence, Charles E. Lawrence Laboratory of Biometrics, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, New York 12237Search for more papers by this authorJeffrey A. Bell, Corresponding Author Jeffrey A. Bell bell@xray.chem.rpi.edu Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180===Search for more papers by this author Swagata Dasgupta, Swagata Dasgupta Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Search for more papers by this authorGanesh H. Iyer, Ganesh H. Iyer Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Search for more papers by this authorStephen H. Bryant, Stephen H. Bryant National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894Search for more papers by this authorCharles E. Lawrence, Charles E. Lawrence Laboratory of Biometrics, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, New York 12237Search for more papers by this authorJeffrey A. Bell, Corresponding Author Jeffrey A. Bell bell@xray.chem.rpi.edu Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, New York 12180Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180===Search for more papers by this author First published: 07 December 1998 https://doi.org/10.1002/(SICI)1097-0134(199708)28:4 3.0.CO;2-ACitations: 116AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract A survey was compiled of several characteristics of the intersubunit contacts in 58 oligomeric proteins, and of the intermolecular contacts in the lattice for 223 protein crystal structures. The total number of atoms in contact and the secondary structure elements involved are similar in the two types of interfaces. Crystal contact patches are frequently smaller than patches involved in oligomer interfaces. Crystal contacts result from more numerous interactions by polar residues, compared with a tendency toward nonpolar amino acids at oligomer interfaces. Arginine is the only amino acid prominent in both types of interfaces. Potentials of mean force for residue–residue contacts at both crystal and oligomer interfaces were derived from comparison of the number of observed residue–residue interactions with the number expected by mass action. They show that hydrophobic interactions at oligomer interfaces favor aromatic amino acids and methionine over aliphatic amino acids; and that crystal contacts form in such a way as to avoid inclusion of hydrophobic interactions. They also suggest that complex salt bridges with certain amino acid compositions might be important in oligomer formation. For a protein that is recalcitrant to crystallization, substitution of lysine residues with arginine or glutamine is a recommended strategy. Proteins 28:494–514, 1997. © 1997 Wiley-Liss, Inc. Citing Literature Volume28, Issue4August 1997Pages 494-514 RelatedInformation