Disulfide bonds Cys9–Cys57, Cys34–Cys88 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-Reference-Cited by-同舟云学术

Disulfide bonds Cys9–Cys57, Cys34–Cys88 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

Published:2003-01 Issue:1 Volume:1645 Page:49-55
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Mishra A.K,Mahale S.D,Iyer K.S

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference21 articles.

1. Disulfide bond mutations affect the folding of the human chorionic gonadotropin-beta subunit in transfected Chinese hamster ovary cells

2. Cystine Knot Mutations Affect the Folding of the Glycoprotein Hormone α-Subunit

3. Glycoprotein Hormones: Structure, Function and Clinical Implications;Keutmann,1994

4. A receptor binding site identified in the region 81–95 of the β-subunit of human luteinizing hormone (LH) and chorionic gonadotropin (hCG)

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