A comprehensive analysis of non-sequential alignments between all protein structures.
Identifieur interne : 001279 ( Main/Exploration ); précédent : 001278; suivant : 001280A comprehensive analysis of non-sequential alignments between all protein structures.
Auteurs : Alexej Abyzov [États-Unis] ; Valentin A. IlyinSource :
- BMC structural biology ; 2007.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Proteins.
- chemical , genetics : Proteins.
- Animals, Databases, Protein, Humans, Protein Structure, Tertiary, Sequence Alignment, Sequence Analysis, Protein, Structural Homology, Protein.
Abstract
The majority of relations between proteins can be represented as a conventional sequential alignment. Nevertheless, unusual non-sequential alignments with different connectivity of the aligned fragments in compared proteins have been reported by many researchers. It is interesting to understand those non-sequential alignments; are they unique, sporadic cases or they occur frequently; do they belong to a few specific folds or spread among many different folds, as a common feature of protein structure. We present here a comprehensive large-scale study of non-sequential alignments between available protein structures in Protein Data Bank.
DOI: 10.1186/1472-6807-7-78
PubMed: 18005453
Affiliations:
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Le document en format XML
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