Structural re-alignment in an immunologic surface region of ricin A chain

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We compared structure alignments generated by several protein structure comparison programs to determine whether existing methods would satisfactorily align residues at a highly conserved position within an immunogenic loop in ribosome inactivating proteins (RIPs). Using default settings, structure alignments generated by several programs (CE, DaliLite, FATCAT, LGA, MAMMOTH, MATRAS, SHEBA, SSM) failed to align the respective conserved residues, although LGA reported correct residue-residue (R-R) correspondences when the beta-carbon (Cb) position was used as the point of reference in the alignment calculations. Further tests using variable points of reference indicated that points distal from the beta carbon along a vector connecting ... continued below

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Zemla, A T & Zhou, C E July 24, 2007.

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We compared structure alignments generated by several protein structure comparison programs to determine whether existing methods would satisfactorily align residues at a highly conserved position within an immunogenic loop in ribosome inactivating proteins (RIPs). Using default settings, structure alignments generated by several programs (CE, DaliLite, FATCAT, LGA, MAMMOTH, MATRAS, SHEBA, SSM) failed to align the respective conserved residues, although LGA reported correct residue-residue (R-R) correspondences when the beta-carbon (Cb) position was used as the point of reference in the alignment calculations. Further tests using variable points of reference indicated that points distal from the beta carbon along a vector connecting the alpha and beta carbons yielded rigid structural alignments in which residues known to be highly conserved in RIPs were reported as corresponding residues in structural comparisons between ricin A chain, abrin-A, and other RIPs. Results suggest that approaches to structure alignment employing alternate point representations corresponding to side chain position may yield structure alignments that are more consistent with observed conservation of functional surface residues than do standard alignment programs, which apply uniform criteria for alignment (i.e., alpha carbon (Ca) as point of reference) along the entirety of the peptide chain. We present the results of tests that suggest the utility of allowing user-specified points of reference in generating alternate structural alignments, and we present a web server for automatically generating such alignments.

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PDF-file: 15 pages; size: 0.3 Mbytes

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  • Journal Name: Bioinformatics and Biology Insights, vol. 2, na, February 1, 2008, pp. 5-13; Journal Volume: 2

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  • Report No.: UCRL-JRNL-233290
  • Grant Number: W-7405-ENG-48
  • Office of Scientific & Technical Information Report Number: 942046
  • Archival Resource Key: ark:/67531/metadc896242

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  • July 24, 2007

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  • Sept. 27, 2016, 1:39 a.m.

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  • Dec. 2, 2016, 12:51 p.m.

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Zemla, A T & Zhou, C E. Structural re-alignment in an immunologic surface region of ricin A chain, article, July 24, 2007; Livermore, California. (digital.library.unt.edu/ark:/67531/metadc896242/: accessed December 10, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.