Abstract
Interaction between S100P and its target protein is an essential step in several cellular functions. The amphiphatic mellitin peptide binds tightly to S100P protein in the presence of calcium cation. Since little is known about the recognition sequence, mellitin interaction form a model for S100P. Interaction between mellitin and protein examined to identify key regions required for the protein-protein interaction.
Keywords: S100P, conformational change, peptide binding
Protein & Peptide Letters
Title: Target Peptide Recognition by S100P Protein and Role of Central Linker Region and Dimer Interface
Volume: 13 Issue: 3
Author(s): Yusuf Tutar
Affiliation:
Keywords: S100P, conformational change, peptide binding
Abstract: Interaction between S100P and its target protein is an essential step in several cellular functions. The amphiphatic mellitin peptide binds tightly to S100P protein in the presence of calcium cation. Since little is known about the recognition sequence, mellitin interaction form a model for S100P. Interaction between mellitin and protein examined to identify key regions required for the protein-protein interaction.
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Cite this article as:
Tutar Yusuf, Target Peptide Recognition by S100P Protein and Role of Central Linker Region and Dimer Interface, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338380
DOI https://dx.doi.org/10.2174/092986606775338380 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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