May 2003
Volume 44, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2003
Homology Modeling of Alpha-crystallin: Analysis of a Conserved N-terminal Structural Motif and its Interaction with the Central Core
Author Affiliations & Notes
  • J.F. Koretz
    Biochemistry Biophysics Prog, Rensselaer Polytech Institute, Troy, NY, United States
  • J.C. Salerno
    Bioinformatics Prog, Rensselaer Polytech Institute, Troy, NY, United States
  • Footnotes
    Commercial Relationships  J.F. Koretz, None; J.C. Salerno, None.
  • Footnotes
    Support  NIH Grant EY10011
Investigative Ophthalmology & Visual Science May 2003, Vol.44, 2373. doi:
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      J.F. Koretz, J.C. Salerno; Homology Modeling of Alpha-crystallin: Analysis of a Conserved N-terminal Structural Motif and its Interaction with the Central Core . Invest. Ophthalmol. Vis. Sci. 2003;44(13):2373.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Abstract: : Purpose: To investigate the functional role and potentially conserved structural motifs of the N-terminal region of alpha-crystallin that precedes the central core, based on analogies to other members of the small heat shock protein superfamily. Methods: Primary sequence alignments of representative samples were initially generated using the programs PILEUP and CLUSTAL W and the pairwise alignment program ALINORM, then further refined manually. The homology model of alphaA-crystallin was derived from the crystallographic structures of methanococcus HSP 16.5 and wheat HSP 16.9.  

Keywords: crystallins • protein structure/function • molecular biology 
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