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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-5-20
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pubmed:abstractText |
The transmembrane precursor of the monkey heparin-binding EGF-like growth factor also functions as a diphtheria toxin receptor. The mouse precursor does not bind the toxin. Previously, the most important region for binding the toxin in the monkey precursor was narrowed down to residues 122-148 through the expression of chimeric mouse/monkey precursors and subsequent toxin-sensitivity assays. To define further the toxin binding domain of the monkey precursor, distinct monkey/mouse chimeric precursors were expressed and assayed. The region between monkey residues 136-148 was found to be absolutely necessary for the retention of toxin sensitivity. Within this region, the monkey and mouse precursors differ in only two residues (residues 141 and 147). A toxin-insensitive monkey/mouse chimera that contained monkey residues 1-136 was converted to a toxin-sensitive chimera by the mutation of a single residue (His141 to Glu141). Expression of a mutant monkey precursor in which a single monkey residue (Glu141) was converted to the mouse residue (His141) yielded a cell line that was approximately 100-fold less sensitive to the toxin and the mutant precursor bound the toxin approximately 12-fold less tightly than the wild-type monkey precursor. Taken together, these results indicate that Glu 141 plays a critical role in toxin binding and toxin sensitivity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
675-80
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8607824-Amino Acid Sequence,
pubmed-meshheading:8607824-Animals,
pubmed-meshheading:8607824-Base Sequence,
pubmed-meshheading:8607824-Binding Sites,
pubmed-meshheading:8607824-DNA Primers,
pubmed-meshheading:8607824-Diphtheria Toxin,
pubmed-meshheading:8607824-Glutamic Acid,
pubmed-meshheading:8607824-Haplorhini,
pubmed-meshheading:8607824-Histidine,
pubmed-meshheading:8607824-Humans,
pubmed-meshheading:8607824-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:8607824-Kinetics,
pubmed-meshheading:8607824-Mice,
pubmed-meshheading:8607824-Molecular Sequence Data,
pubmed-meshheading:8607824-Point Mutation,
pubmed-meshheading:8607824-Polymerase Chain Reaction,
pubmed-meshheading:8607824-Protein Sorting Signals,
pubmed-meshheading:8607824-Receptors, Cell Surface,
pubmed-meshheading:8607824-Recombinant Fusion Proteins,
pubmed-meshheading:8607824-Sequence Homology, Amino Acid
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pubmed:year |
1996
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pubmed:articleTitle |
Glutamic acid 141 of the diphtheria toxin receptor (HB-EGF precursor) is critical for toxin binding and toxin sensitivity.
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pubmed:affiliation |
Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas 75235-9048, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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