Literature DB >> 9796821

Protein structure alignment by incremental combinatorial extension (CE) of the optimal path.

I N Shindyalov1, P E Bourne.   

Abstract

A new algorithm is reported which builds an alignment between two protein structures. The algorithm involves a combinatorial extension (CE) of an alignment path defined by aligned fragment pairs (AFPs) rather than the more conventional techniques using dynamic programming and Monte Carlo optimization. AFPs, as the name suggests, are pairs of fragments, one from each protein, which confer structure similarity. AFPs are based on local geometry, rather than global features such as orientation of secondary structures and overall topology. Combinations of AFPs that represent possible continuous alignment paths are selectively extended or discarded thereby leading to a single optimal alignment. The algorithm is fast and accurate in finding an optimal structure alignment and hence suitable for database scanning and detailed analysis of large protein families. The method has been tested and compared with results from Dali and VAST using a representative sample of similar structures. Several new structural similarities not detected by these other methods are reported. Specific one-on-one alignments and searches against all structures as found in the Protein Data Bank (PDB) can be performed via the Web at http://cl.sdsc.edu/ce.html.

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Substances:

Year:  1998        PMID: 9796821     DOI: 10.1093/protein/11.9.739

Source DB:  PubMed          Journal:  Protein Eng        ISSN: 0269-2139


  651 in total

1.  The Protein Data Bank.

Authors:  H M Berman; J Westbrook; Z Feng; G Gilliland; T N Bhat; H Weissig; I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

2.  Evaluation of PSI-BLAST alignment accuracy in comparison to structural alignments.

Authors:  I Friedberg; T Kaplan; H Margalit
Journal:  Protein Sci       Date:  2000-11       Impact factor: 6.725

3.  CKAAPs DB: a conserved key amino acid positions database.

Authors:  W W Li; B V Reddy; I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2001-01-01       Impact factor: 16.971

4.  A database and tools for 3-D protein structure comparison and alignment using the Combinatorial Extension (CE) algorithm.

Authors:  I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2001-01-01       Impact factor: 16.971

5.  Treble clef finger--a functionally diverse zinc-binding structural motif.

Authors:  N V Grishin
Journal:  Nucleic Acids Res       Date:  2001-04-15       Impact factor: 16.971

6.  Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations.

Authors:  I Tsigelny; I N Shindyalov; P E Bourne; T C Südhof; P Taylor
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

7.  Comparison of sequence profiles. Strategies for structural predictions using sequence information.

Authors:  L Rychlewski; L Jaroszewski; W Li; A Godzik
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

8.  Common fold in helix-hairpin-helix proteins.

Authors:  X Shao; N V Grishin
Journal:  Nucleic Acids Res       Date:  2000-07-15       Impact factor: 16.971

9.  CKAAPs DB: a Conserved Key Amino Acid Positions DataBase.

Authors:  Wilfred W Li; Boojala V B Reddy; John G Tate; Ilya N Shindyalov; Philip E Bourne
Journal:  Nucleic Acids Res       Date:  2002-01-01       Impact factor: 16.971

10.  Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurR.

Authors:  Liskin Swint-Kruse; Christopher Larson; B Montgomery Pettitt; Kathleen Shive Matthews
Journal:  Protein Sci       Date:  2002-04       Impact factor: 6.725

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