The use of folding patterns in a multisolution approach of the all-beta protein three-dimensional structure. A beta-roll structure is predicted in the retroviral glycoprotein.
An automatic macromolecular modelling package of unknown protein structures was developed using the intimate correlation which appears between the observed X-ray structures and their associated predicted folding patterns. The method can be considered as a generalization of both the combinatorial [1] and the template identification [2,3] approaches which were proposed some years ago, and provide a fast way of selecting 'structural motifs' to build new proteins. As an illustration, the tertiary fold of the all-beta-domain of the retroviral outermembrane glycoprotein is proposed.
Busetta
B
B
Laboratoire de cristallographie U.A. 144, Université de Bordeaux, Talence, France.
D000595:Amino Acid Sequence; D002213:Capsid; D004220:Disulfides; D005622:Friend murine leukemia virus; D006023:Glycoproteins; D015368:Human T-lymphotropic virus 1; D015367:Human T-lymphotropic virus 2; D001909:Leukemia Virus, Bovine; D008562:Membrane Glycoproteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008979:Moloney murine leukemia virus; D010447:Peptide Hydrolases; D011487:Protein Conformation; D012191:Retroviridae Proteins; D013816:Thermodynamics
D004220:Disulfides; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D012191:Retroviridae Proteins; D010447:Peptide Hydrolases