Literature DB >> 12217916

The use of structure information to increase alignment accuracy does not aid homologue detection with profile HMMs.

Sam Griffiths-Jones1, Alex Bateman.   

Abstract

MOTIVATION: The best quality multiple sequence alignments are generally considered to derive from structural superposition. However, no previous work has studied the relative performance of profile hidden Markov models (HMMs) derived from such alignments. Therefore several alignment methods have been used to generate multiple sequence alignments from 348 structurally aligned families in the HOMSTRAD database. The performance of profile HMMs derived from the structural and sequence-based alignments has been assessed for homologue detection.
RESULTS: The best alignment methods studied here correctly align nearly 80% of residues with respect to structure alignments. Alignment quality and model sensitivity are found to be dependent on average number, length, and identity of sequences in the alignment. The striking conclusion is that, although structural data may improve the quality of multiple sequence alignments, this does not add to the ability of the derived profile HMMs to find sequence homologues. SUPPLEMENTARY INFORMATION: A list of HOMSTRAD families used in this study and the corresponding Pfam families is available at http://www.sanger.ac.uk/Users/sgj/alignments/map.html CONTACT: sgj@sanger.ac.uk

Mesh:

Year:  2002        PMID: 12217916     DOI: 10.1093/bioinformatics/18.9.1243

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  10 in total

Review 1.  Structural genomics: computational methods for structure analysis.

Authors:  Sharon Goldsmith-Fischman; Barry Honig
Journal:  Protein Sci       Date:  2003-09       Impact factor: 6.725

2.  Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments.

Authors:  Hongyi Zhou; Yaoqi Zhou
Journal:  Proteins       Date:  2005-02-01

3.  Structural similarity to bridge sequence space: finding new families on the bridges.

Authors:  Parantu K Shah; Patrick Aloy; Peer Bork; Robert B Russell
Journal:  Protein Sci       Date:  2005-05       Impact factor: 6.725

4.  Assessing strategies for improved superfamily recognition.

Authors:  Ian Sillitoe; Mark Dibley; James Bray; Sarah Addou; Christine Orengo
Journal:  Protein Sci       Date:  2005-06-03       Impact factor: 6.725

Review 5.  Exploiting protein structure data to explore the evolution of protein function and biological complexity.

Authors:  Russell L Marsden; Juan A G Ranea; Antonio Sillero; Oliver Redfern; Corin Yeats; Michael Maibaum; David Lee; Sarah Addou; Gabrielle A Reeves; Timothy J Dallman; Christine A Orengo
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2006-03-29       Impact factor: 6.237

6.  Simple chained guide trees give high-quality protein multiple sequence alignments.

Authors:  Kieran Boyce; Fabian Sievers; Desmond G Higgins
Journal:  Proc Natl Acad Sci U S A       Date:  2014-07-07       Impact factor: 11.205

7.  Automatic assessment of alignment quality.

Authors:  Timo Lassmann; Erik L L Sonnhammer
Journal:  Nucleic Acids Res       Date:  2005-12-16       Impact factor: 16.971

8.  Application of protein structure alignments to iterated hidden Markov model protocols for structure prediction.

Authors:  Eric D Scheeff; Philip E Bourne
Journal:  BMC Bioinformatics       Date:  2006-09-14       Impact factor: 3.169

9.  Improving model construction of profile HMMs for remote homology detection through structural alignment.

Authors:  Juliana S Bernardes; Alberto M R Dávila; Vítor S Costa; Gerson Zaverucha
Journal:  BMC Bioinformatics       Date:  2007-11-09       Impact factor: 3.169

Review 10.  Recent evolutions of multiple sequence alignment algorithms.

Authors:  Cédric Notredame
Journal:  PLoS Comput Biol       Date:  2007-08       Impact factor: 4.475

  10 in total

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