Structural updates of alignment of protein domains and consequences on evolutionary models of domain superfamilies.

ABSTRACT:

Background

Influx of newly determined crystal structures into primary structural databases is increasing at a rapid pace. This leads to updation of primary and their dependent secondary databases which makes large scale analysis of structures even more challenging. Hence, it becomes essential to compare and appreciate replacement of data and inclusion of new data that is critical between two updates. PASS2 is a database that retains structure-based sequence alignments of protein domain superfamilies and relies on SCOP database for its hierarchy and definition of superfamily members. Since, accurate alignments of distantly related proteins are useful evolutionary models for depicting variations within protein superfamilies, this study aims to trace the changes in data in between PAS

SUBMITTER: Mutt E 

PROVIDER: S-EPMC4175504 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature