Relaxin and its structural relationship to insulin
| Autor: | Neil Isaacs, Guy Dodson, Hugh D. Niall, Alan Evans, Anthony C.T. North, Gillian D. Bryant-Greenwood, Robert B. James |
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| Rok vydání: | 1978 |
| Předmět: |
Models
Molecular endocrine system medicine.medical_specialty Protein Conformation medicine.medical_treatment Cystine Peptide Homology (biology) Structure-Activity Relationship chemistry.chemical_compound Internal medicine medicine Insulin Amino Acid Sequence Disulfides Relaxin chemistry.chemical_classification Multidisciplinary Computers urogenital system Chemistry Tryptophan medicine.anatomical_structure Endocrinology Pancreas Corpus luteum hormones hormone substitutes and hormone antagonists Hormone |
| Zdroj: | Nature. 271:278-281 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | THE sequence of the ovarian peptide, relaxin, has recently been reported1,2 and the observation1 that it can be accommodated into the insulin fold has been discussed3,4. Only 11 residues, including the cystines, are common to insulin and relaxin (Fig. 1), but the probable identity of the cystine pairings and the preservation of the hydrophobic character of buried residues suggests some structural homology between the two hormones. The extent of sequence changes and the remote relationship between the corpus luteum and the pancreas, the respective sources of relaxin and insulin, makes homology of the two hormones most interesting. We have therefore rigorously examined the relaxin conformation by a computer graphics system and found it possible to accommodate the relaxin sequence within the insulin main-chain geometry. |
| Databáze: | OpenAIRE |
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