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Secondary structure and solvent accessibilityEdit
The prediction of p53 secondary structure and solvent accessibility was obtained using PredictProtein. The results show a primarily looped structure (71.25%) containing a small amount of α–helices (12.21%) and β–sheets (16.54%).
p53 seems to have varying solvent accessibility. The majority of the protein’s surface area appears to be in a buried state (45.25%) or has intermediate accessibility (18.07%), while only a small amount (36.64%) of the protein appears to be exposed and readily accessible to solvents.
The structure predicted by PredictProtein is similar to the actual secondary structure analyzed by the PDBeView here. The secondary structural elements in p53 were determined by studying the p53 tetramer and analyzing the composition (strand, helix, and "other") of each monomer (shown in chains). The analysis shows a composition appearing consistent with the PredictProtein analysis, and appears to be little structural variation between chains.
P53 is a tetramer composed of four identical protein chains. The p53 tetramer binds response elements in target genes with the consensus motif, activating expression of target proteins. Two p53 dimers assemble on the consensus motif to form the tetramer
Of the several domains that compose p53, three have been studied extensively.
The first of these domains is the tetramerization domain, located at the center of the protein. This domain is responsible for connecting the four protein chains. Each chain connects to the DNA–binding domain. The third domain that has been studied is the transactivation domain, which is located near the end of each arm. The transactivation domain is responsible for activating DNA–reading machinery.
- Prediction of secondary structure and solvent accessibility: from PredictProtein.org
- Further structural information from:
- Keri: p53: Introduction
- Keri: p53: Biological function
- Keri: p53: Biosynthesis
- Keri: p53: Gene sequence
- Keri: p53: Amino acid sequence and composition
- Keri: p53: Secondary and tertiary structure
- Keri: p53: Domains and structural motifs
- Keri: p53: Interactions with macromolecules and small molecules
- Keri: p53: Molecular biodiversity and evolution
- Keri: p53: Literature overview
- Keri: p53: Useful online resources