Superdomains in the protein structure hierarchy: The case of PTP‐C2
| Autor: | Donald T. Haynie, Bin Xue |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular animal structures Protein tyrosine phosphatase environment and public health Biochemistry Conserved sequence law.invention Domain interface Protein structure law Catalytic Domain Animals Humans PTEN Amino Acid Sequence Casein Kinase II Molecular Biology Conserved Sequence C2 domain Genetics chemistry.chemical_classification Sequence Homology Amino Acid biology Fungi PTEN Phosphohydrolase Articles Plants Protein Structure Tertiary Amino acid enzymes and coenzymes (carbohydrates) chemistry biology.protein Suppressor Protein Tyrosine Phosphatases Protein Binding |
| Zdroj: | Protein Science. 24:874-882 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.2664 |
| Popis: | Superdomain is uniquely defined in this work as a conserved combination of different globular domains in different proteins. The amino acid sequences of 25 structurally and functionally diverse proteins from fungi, plants, and animals have been analyzed in a test of the superdomain hypothesis. Each of the proteins contains a protein tyrosine phosphatase (PTP) domain followed by a C2 domain. Four novel conserved sequence motifs have been identified, one in the PTP domain and three in the C2 domain. All contribute to the PTP-C2 domain interface in PTEN, a tumor suppressor, and all are more conserved than the PTP signature motif, HCX3 (K/R)XR, in the 25 sequences. We show that PTP-C2 was formed prior to the fungi, plant, and animal kingdom divergence. A superdomain as defined here does not fit the usual protein structure classification system. The demonstrated existence of one superdomain suggests the existence of others. |
| Databáze: | OpenAIRE |
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