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A data bank merging related protein structures and sequences.

S Pascarella¹, P Argos

¹European Molecular Biology Laboratory, Heidelberg, Germany.

Protein Engineering

|March 1, 1992

Summary

This study merges protein structural and sequence data, creating a larger database. This integration significantly expands sequence entries linked to known 3D protein structures.

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Area of Science:

Structural biology
Bioinformatics
Protein science

Background:

Protein structure and sequence data are crucial for understanding biological function.
Integrating diverse data sources can enhance biological databases.

Purpose of the Study:

To create a comprehensive data collection merging protein structural and sequence information.
To increase the number of sequence entries associated with known three-dimensional protein architectures.

Main Methods:

Performed structural superpositions for proteins with similar main-chain folds.
Associated protein primary sequences with multiple structural alignments based on homology thresholds (≥50% residue identity and alignability).
Collected data for 38 familial groups (209 tertiary structures) and 45 individual structures, including conformational angles and secondary structure assignments.

Main Results:

Successfully merged protein structural and sequence data.
Achieved an 8-fold increase in data bank sequence entries compared to using only 3D architectures.
Established confidence in primary sequence conformation relative to tertiary structural templates, acknowledging variations in loop regions.

Conclusions:

The integrated database significantly enhances the utility of protein sequence information.
Merging structural and sequence data provides a more complete resource for biological research.
This approach offers a powerful method for expanding and enriching protein databases.

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