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Published on: May 26, 2011
Divergence of interdomain geometry in two-domain proteins
Jung-Hoon Han1, Nicola Kerrison, Cyrus Chothia
1MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, United Kingdom. jhh03@mrc-lmb.cam.ac.uk
Structure (London, England : 1993)
|May 16, 2006
Summary
Homologous proteins often maintain their domain structure and interface geometry. However, some proteins exhibit variable geometries and interface structures despite high sequence identity, indicating evolutionary flexibility.
Area of Science:
- Structural biology
- Protein biochemistry
- Bioinformatics
Background:
- Homologous proteins can consist of multiple domains.
- The spatial arrangement (geometry) and interaction (interface) of these domains are crucial for protein function.
- Understanding the conservation of these features is key to deciphering protein evolution and function.
Purpose of the Study:
- To investigate the conservation of interdomain geometry and domain interface structure in homologous two-domain proteins.
- To identify factors influencing the variability observed in these structural features.
Main Methods:
- Analysis of 128 unique two-domain protein architectures.
- Comparison of interdomain geometry and domain interface structures across homologous proteins.
- Correlation of structural variations with interface properties and sequence identity.
Main Results:
- 75 out of 128 architectures conserved both interdomain geometry and interface structure.
- 5 architectures conserved geometry but not interface structure.
- 48 architectures showed variable geometries and divergent interface structures.
- Interface changes or absence of an interface were linked to geometric variations.
- Variable geometries were observed even in homologous proteins with high sequence identities (up to 70%).
Conclusions:
- Interdomain geometry and interface structure conservation varies significantly among homologous proteins.
- Protein interfaces play a critical role in maintaining or altering interdomain geometry.
- High sequence identity does not guarantee conserved interdomain geometry, highlighting structural plasticity in protein evolution.
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