Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor. [electronic resource]
Producer: 20011205Description: 5543-55 p. digitalISSN:- 0261-4189
- Animals
- Binding Sites
- Cell Line
- Crystallography, X-Ray
- Dimerization
- Dogs
- Drug Design
- Heparin -- chemistry
- Heparitin Sulfate -- metabolism
- Hepatocyte Growth Factor -- chemistry
- Humans
- Kidney
- Kringles
- Macromolecular Substances
- Models, Molecular
- Mutagenesis, Site-Directed
- Peptide Fragments -- chemistry
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- Proto-Oncogene Proteins c-met -- antagonists & inhibitors
- RNA Splicing
- Recombinant Fusion Proteins -- chemistry
- Structure-Activity Relationship
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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