Abstract
Protein structures were collected from the Brookhaven Database of tertiary architectures that displayed oligomeric association (24 molecules) or whose polypeptide folding revealed domains (34 proteins). The subunit and domain interfaces for these proteins were respectively examined from the following aspects: percentage water-accessible surface area buried by the respective associations, surface compositions and physical characteristics of the residues involved in the subunit and domain contacts, secondary structural state of the interface amino acids, preferred polar and non-polar interactions, spatial distribution of polar and non-polar residues on the interface surface, same residue interactions in the oligomeric contacts, and overall cross-section and shape of the contact surfaces. A general, consistent picture emerged for both the domain and subunit interfaces.
Keywords
Protein subunitDomain (mathematical analysis)Library scienceSelection (genetic algorithm)Computer scienceBiologyInformation retrievalGeneticsMathematicsArtificial intelligenceGene
Related Publications
Protein–protein interaction at crystal contacts
Abstract Packing contacts are crystal artifacts, yet they make use of the same forces that govern specific recognition in protein‐protein complexes and oligomeric proteins. They...
Automatic inference of protein quaternary structure from crystals
The arrangement of the subunits in an oligomeric protein often cannot be inferred without ambiguity from crystallographic studies. The annotation of the functional assembly of p...
Dissecting protein–protein recognition sites
Abstract The recognition sites in 70 pairwise protein–protein complexes of known three‐dimensional structure are dissected in a set of surface patches by clustering atoms at the...
Protein-Protein Interfaces: Architectures and Interactions in Protein-Protein Interfaces and in Protein Cores. Their Similarities and Differences
Protein structures generally consist of favorable folding motifs formed by specific arrangements of secondary structure elements. Similar architectures can be adopted by differe...
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
MolProbity is a general-purpose web server offering quality validation for 3D structures of proteins, nucleic acids and complexes. It provides detailed all-atom contact analysis...
Publication Info
- Year
- 1988
- Type
- article
- Volume
- 2
- Issue
- 2
- Pages
- 101-113
- Citations
- 207
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
207
OpenAlex
Cite This
Patrick Argos
(1988).
An investigation of protein subunit and domain interfaces.
Protein Engineering Design and Selection
, 2
(2)
, 101-113.
https://doi.org/10.1093/protein/2.2.101
Identifiers
- DOI
- 10.1093/protein/2.2.101