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Titolo:
SECONDARY STRUCTURE PREDICTION OF BETA-SUBUNITS OF THE GONADOTROPIN-THYROTROPIN FAMILY FROM ITS ALIGNED SEQUENCES USING ENVIRONMENT-DEPENDENT AMINO-ACID SUBSTITUTION TABLES AND CONFORMATIONAL PROPENSITIES
Autore:
WAKO H; ISHII S;
Indirizzi:
WASEDA UNIV,SCH SOCIAL SCI,SHINJUKU KU,1-6-1 NISHI WASEDA TOKYO 16950JAPAN WASEDA UNIV,SCH EDUC,DEPT BIOL,SHINJUKU KU TOKYO 16950 JAPAN
Titolo Testata:
Biochimica et biophysica acta. Protein structure and molecular enzymology
fascicolo: 1, volume: 1247, anno: 1995,
pagine: 104 - 112
SICI:
0167-4838(1995)1247:1<104:SSPOBO>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN LUTEINIZING-HORMONE; HUMAN CHORIONIC-GONADOTROPIN; RECEPTOR-BINDING REGION; TERTIARY STRUCTURE; PEPTIDES; ALIGNMENT; DIVERGENCE; INHIBITION; PROTEINS; RESIDUES;
Keywords:
SECONDARY STRUCTURE PREDICTION; AMINO-ACID SUBSTITUTION TABLES; GONADOTROPIN; THYROTROPIN; LUTEINIZING HORMONE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
H. Wako e S. Ishii, "SECONDARY STRUCTURE PREDICTION OF BETA-SUBUNITS OF THE GONADOTROPIN-THYROTROPIN FAMILY FROM ITS ALIGNED SEQUENCES USING ENVIRONMENT-DEPENDENT AMINO-ACID SUBSTITUTION TABLES AND CONFORMATIONAL PROPENSITIES", Biochimica et biophysica acta. Protein structure and molecular enzymology, 1247(1), 1995, pp. 104-112

Abstract

The secondary structures of beta-subunits of the glycoprotein hormonefamily, LH (luteinizing hormone), CG (chorionic gonadotropin), FSH (follicle stimulating hormone), TSH (thyroid stimulating hormone), and GTH I/GTH II (two types of fish gonadotropins), are predicted by comparing an amino-acid substitution pattern at equivalent sites in their aligned sequences with environment-dependent amino-acid substitution tables and conformational propensities calculated from other protein families whose three-dimensional structures are known. According to the prediction results, together with other structural information obtained from experiments, the following points come up as important structuralfeatures of the beta-subunits of this family; The regions assigned toregular secondary structures (one alpha-helix and three beta-strands)are considered to constitute a core of the beta-subunits. They involve interaction sites with carbohydrate and alpha-subunit. Out of the six disulfide bonds formed in the beta-subunit, four are located together on one side of the core, and the other two on the opposite side. Thetwo regions assumed to be a receptor binding region from experiments (therefore, species-specific regions) are predicted as loops located on the same side of the beta-subunit in this study. Some of the predicted loops are rich in proline residues. While the positions of proline residues are conserved in the family generally, there are hormone- or species-specific ones in the loop that is assumed to take part in receptor binding. The possible importance of proline residues in hormone or species specificity is discussed. (After submitting the manuscript the X-ray crystal structure of human CG was published. In order to evaluate the prediction, the original manuscript is kept intact and a comparison has been made between the prediction results and the crystal structure in an appendix)

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Documento generato il 01/12/20 alle ore 07:32:05