Premium
Using physical models of proteins to tell molecular stories of research‐based health care
Author(s) -
Herman Tim,
Deboer Karen,
LaFlamme Donna,
Franzen Margaret,
Goodsell David
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a976-d
Subject(s) - active site , catalytic triad , hemagglutinin (influenza) , substrate (aquarium) , acetylcholine , chemistry , acetylcholinesterase , fusion protein , biophysics , computational biology , virus , biochemistry , biology , enzyme , virology , gene , recombinant dna , ecology , endocrinology
Physical models of proteins are powerful new instructional tools that can be used to tell complex molecular stories. The models, based on the atomic coordinates of solved structures, are designed using a modified version of RasMol and constructed using rapid prototyping technologies. Two models of current interest include: The Influenza HA (Hemagglutinin) Protein : This protein catalyzes membrane fusion during influenza virus infection. We have created an alpha carbon backbone model of this protein to highlight the different mutations that have occurred to produce the highly pathogenic 1918 pandemic strain of this virus as well as the current H5N1 strain. A second model of this protein highlights the conformational changes that occur in this protein to facilitate membrane fusion. The Active Site of Acetylcholinesterase : Acetylcholinesterase cleaves the acetylcholine neurotransmitter and thereby restores a synapse to its resting state. This spacefilled model of the active site features the catalytic triad (Ser, His and Glu) that catalyzes the reaction and a model of the acetylcholine substrate that can be docked into the active site. The binding of an organophosphate insecticide at a site adjacent to the substrate binding site can be shown to block substrate binding, leading to inhibition of the enzyme. This work is supported by an NIH NCRR SEPA grant and an NSF DUE CCLI award.