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The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments
1Graduate School of Information Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Bioinformation
|March 3, 2017
Summary
Intrinsically disordered proteins (IDPs) feature protean segments (ProSs) that transition from disorder to order upon partner binding. Analysis reveals distinct structural differences between ProSs and heterodimers, with irregular structures playing a key role in binding interactions.
Area of Science:
- Biochemistry
- Structural Biology
- Computational Biology
Background:
- Intrinsically disordered proteins (IDPs) lack stable structures but are crucial for biological functions.
- Protean segments (ProSs) are functional IDP regions that adopt ordered structures upon binding.
- The IDEAL database provides annotated ProSs for analysis.
Purpose of the Study:
- To classify and analyze the secondary structure elements (SSEs) at the interface of ProSs.
- To compare the amino acid composition and solvent accessibility of ProS interfaces with heterodimers.
- To investigate the relationship between structural features and binding efficiency of ProSs.
Main Methods:
- Classification of ProS interfaces into core, rim, and support regions.
- Analysis of secondary structure elements (SSEs) using relative accessible surface area (rASA).
- Comparison of amino acid composition, rASA, and contact numbers between ProSs and heterodimers.
Main Results:
- Significant differences in irregular structures were observed between ProSs and heterodimers.
- Larger relative solvent accessible surface area (rASA) in the monomeric state (rASAm) of irregular structures correlates with increased binding contacts.
- ProSs were successfully classified into high and low efficiency groups based on interface contact numbers.
Conclusions:
- Irregular structures are critical determinants of ProS function and binding.
- The disorder-to-order transition in ProSs is driven by specific structural and chemical properties at the interface.
- Understanding these structural dynamics provides insights into IDP-mediated biological processes.
Keywords:
Intrinsically disordered proteinsprotean segments (ProSs)protein interfaceprotein-protein interactionsrelative solvent accessible surface area (rASA)secondary structure elements (SSEs)More Related Videos
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