Disulfide bonds Cys9-Cys57, Cys34-Cys 88 and Cys38-Cys90 of the β-subunit of human chorionic gonadotropin are crucial for heterodimer formation with the α-subunit: Experimental evidence for the conclusions from the crystal structure of hCG

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1645, Issue 1, 2003, Pages 49-55

  Mishra, A K ^a   Mahale, S D ^b   Iyer, K S ^b  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b NATIONAL INSTITUTE FOR RESEARCH IN REPRODUCTIVE HEALTH   (India)

Author keywords

Disulfide peptide; Heterodimer formation; Human chorionic gonadotropin; Role of disulfide bond

Indexed keywords

CHORIONIC GONADOTROPIN; CYSTEINE; DISULFIDE; CHORIONIC GONADOTROPIN BETA SUBUNIT; PEPTIDE FRAGMENT;

ALPHA CHAIN; ARTICLE; BETA CHAIN; COMPETITIVE INHIBITION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME INHIBITION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN STABILITY; SCREENING TEST; AMINO ACID SEQUENCE; BINDING COMPETITION; CHEMISTRY; CRYSTALLIZATION; DIMERIZATION; GENETIC RECOMBINATION; HUMAN; MOLECULAR GENETICS; SYNTHESIS;

AMINO ACID SEQUENCE; BINDING, COMPETITIVE; CHORIONIC GONADOTROPIN, BETA SUBUNIT, HUMAN; CRYSTALLIZATION; DIMERIZATION; DISULFIDES; GLYCOPROTEIN HORMONES, ALPHA SUBUNIT; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; RECOMBINATION, GENETIC;

EID: 1242317842     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00501-0     Document Type: Article

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