Structural similarity of loops in protein families: toward the understanding of protein evolution.
BACKGROUND
Protein evolution and protein classification are usually inferred by comparing protein cores in their conserved aligned parts. Structurally aligned protein regions are separated by less conserved loop regions, where sequence and structure locally deviate from each other and do not superimpose well.


RESULTS
Our results indicate that even longer protein loops can not be viewed as "random coils" and for the majority of protein families in our test set there exists a linear correlation between the measures of sequence similarity and loop structural similarity. Results suggest that distance matrices derived from the loop (dis)similarity measure may produce in some cases more reliable cluster trees compared to the distance matrices based on the conventional measures of sequence and structural (dis)similarity.


CONCLUSIONS
We show that by considering "dissimilar" loop regions rather than only conserved core regions it is possible to improve our understanding of protein evolution.
Panchenko
Anna R
AR
Computational Biology Branch, National Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894, USA. panch@ncbi.nlm.nih.gov
Madej
Thomas
T
D000465:Algorithms; D000818:Animals; D005075:Biological Evolution; D016000:Cluster Analysis; D019143:Evolution, Molecular; D017353:Gene Deletion; D008040:Genetic Linkage; D023281:Genomics / Q000379:methods; D008957:Models, Genetic; D008958:Models, Molecular; D015233:Models, Statistical; D009154:Mutation; D010802:Phylogeny; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D012259:Ribonuclease, Pancreatic / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment
D011506:Proteins; D012259:Ribonuclease, Pancreatic