Crystal structure of human chorionic gonadotropin
| Autor: | D. C. Harris, Allison Littlejohn, Neil W. Isaacs, R. E. Canfield, J. W. Lustbader, K. J. Machin, F. J. Morgan, Adrian J. Lapthorn |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Folding Stereochemistry Protein Conformation Protein subunit Molecular Sequence Data Biology Crystallography X-Ray Chorionic Gonadotropin Protein structure Carbohydrate Conformation Computer Graphics Humans Amino Acid Sequence Disulfides Binding site Growth Substances Peptide sequence Glycoproteins Multidisciplinary Cystine knot Receptors LH Hormones Folding (chemistry) Cystine Protein folding Carbohydrate conformation |
| Zdroj: | Nature. 369(6480) |
| ISSN: | 0028-0836 |
| Popis: | The three-dimensional structure of human chorionic gonadotropin shows that each of its two different subunits has a similar topology, with three disulphide bonds forming a cystine knot. This same folding motif is found in some protein growth factors. The heterodimer is stabilized by a segment of the beta-subunit which wraps around the alpha-subunit and is covalently linked like a seat belt by the disulphide Cys 26-Cys 110. This extraordinary feature appears to be essential not only for the association of these heterodimers but also for receptor binding by the glycoprotein hormones. |
| Databáze: | OpenAIRE |
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