Nerve growth factor: Structure/function relationships
| Autor: | Judith Murray-Rust, Carlos F. Ibáñez, R. Lapatto, Tom L. Blundell, Neil Q. McDonald, Ralph A. Bradshaw |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Protein Conformation Dimer Molecular Sequence Data Sequence alignment Receptors Nerve Growth Factor Biology Crystallography X-Ray Biochemistry Protein Structure Secondary chemistry.chemical_compound Protein structure Computer Graphics Animals Humans Amino Acid Sequence Nerve Growth Factors Molecular Biology Peptide sequence Conserved Sequence Mutagenesis Protein tertiary structure Protein Structure Tertiary Nerve growth factor chemistry Mutagenesis Site-Directed Biophysics Protein quaternary structure Sequence Alignment Research Article |
| Zdroj: | Protein Science. 3:1901-1913 |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | Nerve growth factor (NGF), which has a tertiary structure based on a cluster of 3 cystine disulfides and 2 very extended, but distorted beta-hairpins, is the prototype of a larger family of neurotrophins. Prior to the availability of cloning techniques, the mouse submandibular gland was the richest source of NGF and provided sufficient material to enable its biochemical characterization. It binds as a dimer to at least 2 cell-surface receptor types expressed in a variety of neuronal and non-neuronal cells. Residues involved in these interactions and in the maintenance of tertiary and quaternary structure have been identified by chemical modification and site-directed mutagenesis, and this information can be related to their location in the 3-dimensional structure. For example, interactions between aromatic residues contribute to the stability of the NGF dimer, and specific surface lysine residues participate in receptor contacts. The conclusion from these studies is that receptor interactions involve broad surface regions, which may be composed of residues from both promoters in the dimer. |
| Databáze: | OpenAIRE |
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