HOMSTRAD

Mizuguchi, K., Deane, C. M., Blundell, T. L., and Overington, J. P. (1998) HOMSTRAD a database of protein structure alignments for homologous families. 

View Ranking (Click on a profile liit will bring you to the corresponding HOMSTRAD family)... 

As mentioned above, several of these approaches have been employed to generate exhaustive clusterings of the protein structures into structural classes available via the resulting databases (DDD/FSSP/Dali [102], 3Dee [79], JOY/HOMSTRAD/DDBASE [112-114], structure cores LPFC [115]), These superposition-based classifications are complemented with classi-... 

HOMSTRAD Database of structure based alignments http // www-c17st.bioc.cam.ac.uk/ homstrad/ K. Mizuguchi et al. [112]... 

Library of profiles and substitution matrices from HOMSTRAD structural alignment DB. Sequence or profile is searched against library. 

An analysis of the HOMSTRAD database showed that the PP II conformation represents 3% of the all peptide conformations and even occurs in 1.3% of peptides when only helices consisting of more than three residues are considered [106]. Proline is greatly favored in PP II helices, whereas Gly and aromatic amino acids have low propensity for the PP II structure. It is worth noting that although Gly generally disfavors the PP II helix, it is common in collagen. Collagen consists... 

HOMSTRAD http //www-cryst.bioc.cam.ac.uk/homstrad Homologous struct alignments... 

The PROSITE database is used to determine the domain and the family of the protein sequences that, in turn, are based on biologically significant sites, patterns, and profiles.This database is similar to the HOMologous STRucture Alignment Database " (HOMSTRAD) and the Protein family (Pfam) database, both of which contain domain and family information for proteins. HOMSTRAD uses sequence and structure to group proteins into domains and families. Pfam classifies protein domains and families, based... 

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