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Secondary structure prediction and unrefined tertiary structure prediction for cyclin A, B, and D
Author(s) -
Gerloff Dietlind L.,
Cohen Fred E.
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199601)24:1<18::aid-prot2>3.0.co;2-k
Subject(s) - protein tertiary structure , cyclin dependent kinase , cyclin , protein secondary structure , computational biology , heuristics , sequence (biology) , protein structure , phosphorylation , biology , chemistry , computer science , crystallography , stereochemistry , biochemistry , cell cycle , cell , operating system
We present heuristic‐based predictions of the secondary and tertiary structures of the cyclins A, B, and D, representatives of the cyclin superfamily. The list of suggested constraints for tertiary structure assembly was left unrefined in order to submit this report before an announced crystal structure for cyclin A becomes available. To predict these constraints, a master sequence alignment over 270 positions of cyclin types A, B, and D was adjusted based on individual secondary structure predictions for each type. We used new heuristics for predicting aromatic residues at protein‐protein interfaces and to identify sequentially distinct regions in the protein chain that cluster in the folded structure. The boundaries of two conjectured domains in the cyclin fold were predicted based on experimental data in the literature. The domain that is important for interaction of the cyclins with cyclin‐dependent kinases (CDKs) is predicted to contain six helices; the second domain in the consensus model contains both helices and a β‐sheet that is formed by sequentially distant regions in the protein chain. A plausible phosphorylation site is identified. This work represents a blinded test of the method for prediction of secondary and, to a lesser extent, tertiary structure from a set of homologous protein sequences. Evaluation of our predictions will become possible with the publication of the announced crystal structure.