A proposed structural model of domain 1 of fasciclin III neural cell adhesion protein based on an inverse folding algorithm
| Autor: | Jacquelyn S. Fetrow, Stephen H. Bryant, Peter M. Snow, Laurie A. Castonguay |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Protein Folding Protein Conformation Globular protein Cell Adhesion Molecules Neuronal Molecular Sequence Data Immunoglobulins Biology Biochemistry Domain (software engineering) Protein sequencing Molecular recognition Animals Drosophila Proteins Computer Simulation Amino Acid Sequence Homology modeling Molecular Biology Integral membrane protein chemistry.chemical_classification Sequence Homology Amino Acid Protein structure prediction Peptide Fragments chemistry CD4 Antigens Immunoglobulin superfamily Drosophila Algorithm Algorithms Research Article |
| Zdroj: | Protein Science. 4:472-483 |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | Fasciclin III is an integral membrane protein expressed on a subset of axons in the developing Drosophila nervous system. It consists of an intracellular domain, a transmembrane region, and an extracellular region composed of three domains, each predicted to form an immunoglobulin-like fold. The most N-terminal of these domains is expected to be important in mediating cell-cell recognition events during nervous system development. To learn more about the structure/function relationships in this cellular recognition molecule, a model structure of this domain was built. A sequence-to-structure alignment algorithm was used to align the protein sequence of the fasciclin III first domain to the immunoglobulin McPC603 structure. Based on this alignment, a model of the domain was built using standard homology modeling techniques. Side-chain conformations were automatically modeled using a rotamer search algorithm and the model was minimized to relax atomic overlaps. The resulting model is compact and has chemical characteristics consistent with related globular protein structures. This model is a de novo test of the sequence-to-structure alignment algorithm and is currently being used as the basis for mutagenesis experiments to discern the parts of the fasciclin III protein that are necessary for homophilic molecular recognition in the developing Drosophila nervous system. |
| Databáze: | OpenAIRE |
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