@article{RN208,
   author = {Xiao, S. and Charonko, J. J. and Fu, X. and Salmanzadeh, A. and Davalos, R. V. and Vlachos, P. P. and Finkielstein, C. V. and Capelluto, D. G.},
   title = {Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide},
   journal = {J Biol Chem},
   volume = {287},
   number = {45},
   pages = {37691-702},
   note = {1083-351x
Xiao, Shuyan
Charonko, John J
Fu, Xiangping
Salmanzadeh, Alireza
Davalos, Rafael V
Vlachos, Pavlos P
Finkielstein, Carla V
Capelluto, Daniel G S
Journal Article
Research Support, Non-U.S. Gov't
United States
2012/09/15
J Biol Chem. 2012 Nov 2;287(45):37691-702. doi: 10.1074/jbc.M112.385609. Epub 2012 Sep 13.},
   abstract = {Disabled-2 (Dab2) targets membranes and triggers a wide range of biological events, including endocytosis and platelet aggregation. Dab2, through its phosphotyrosine-binding (PTB) domain, inhibits platelet aggregation by competing with fibrinogen for α(IIb)β(3) integrin receptor binding. We have recently shown that the N-terminal region, including the PTB domain (N-PTB), drives Dab2 to the platelet membrane surface by binding to sulfatides through two sulfatide-binding motifs, modulating the extent of platelet aggregation. The three-dimensional structure of a Dab2-derived peptide encompassing the sulfatide-binding motifs has been determined in dodecylphosphocholine micelles using NMR spectroscopy. Dab2 sulfatide-binding motif contains two helices when embedded in micelles, reversibly binds to sulfatides with moderate affinity, lies parallel to the micelle surface, and when added to a platelet mixture, reduces the number and size of sulfatide-induced aggregates. Overall, our findings identify and structurally characterize a minimal region in Dab2 that modulates platelet homotypic interactions, all of which provide the foundation for rational design of a new generation of anti-aggregatory low-molecular mass molecules for therapeutic purposes.},
   keywords = {Adaptor Proteins, Signal Transducing/*chemistry/genetics/metabolism
Amino Acid Motifs
Amino Acid Sequence
Apoptosis Regulatory Proteins
Binding Sites
Circular Dichroism
Humans
Micelles
Models, Molecular
Molecular Sequence Data
Peptides/*chemistry/metabolism/*pharmacology
Phosphorylcholine/analogs & derivatives/chemistry
Platelet Adhesiveness/drug effects
Platelet Aggregation/*drug effects
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Sulfoglycosphingolipids/*chemistry/metabolism
Surface Plasmon Resonance
Tumor Suppressor Proteins/*chemistry/genetics/metabolism},
   ISSN = {0021-9258 (Print)
0021-9258},
   DOI = {10.1074/jbc.M112.385609},
   year = {2012},
   type = {Journal Article}
}

{"_id":"7vXAe2JHL9qL5AQaF","bibbaseid":"xiao-charonko-fu-salmanzadeh-davalos-vlachos-finkielstein-capelluto-structuresulfatidebindingpropertiesandinhibitionofplateletaggregationbyadisabled2proteinderivedpeptide-2012","author_short":["Xiao, S.","Charonko, J. J.","Fu, X.","Salmanzadeh, A.","Davalos, R. V.","Vlachos, P. P.","Finkielstein, C. V.","Capelluto, D. G."],"bibdata":{"bibtype":"article","type":"Journal Article","author":[{"propositions":[],"lastnames":["Xiao"],"firstnames":["S."],"suffixes":[]},{"propositions":[],"lastnames":["Charonko"],"firstnames":["J.","J."],"suffixes":[]},{"propositions":[],"lastnames":["Fu"],"firstnames":["X."],"suffixes":[]},{"propositions":[],"lastnames":["Salmanzadeh"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Davalos"],"firstnames":["R.","V."],"suffixes":[]},{"propositions":[],"lastnames":["Vlachos"],"firstnames":["P.","P."],"suffixes":[]},{"propositions":[],"lastnames":["Finkielstein"],"firstnames":["C.","V."],"suffixes":[]},{"propositions":[],"lastnames":["Capelluto"],"firstnames":["D.","G."],"suffixes":[]}],"title":"Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide","journal":"J Biol Chem","volume":"287","number":"45","pages":"37691-702","note":"1083-351x Xiao, Shuyan Charonko, John J Fu, Xiangping Salmanzadeh, Alireza Davalos, Rafael V Vlachos, Pavlos P Finkielstein, Carla V Capelluto, Daniel G S Journal Article Research Support, Non-U.S. Gov't United States 2012/09/15 J Biol Chem. 2012 Nov 2;287(45):37691-702. doi: 10.1074/jbc.M112.385609. Epub 2012 Sep 13.","abstract":"Disabled-2 (Dab2) targets membranes and triggers a wide range of biological events, including endocytosis and platelet aggregation. Dab2, through its phosphotyrosine-binding (PTB) domain, inhibits platelet aggregation by competing with fibrinogen for α(IIb)β(3) integrin receptor binding. We have recently shown that the N-terminal region, including the PTB domain (N-PTB), drives Dab2 to the platelet membrane surface by binding to sulfatides through two sulfatide-binding motifs, modulating the extent of platelet aggregation. The three-dimensional structure of a Dab2-derived peptide encompassing the sulfatide-binding motifs has been determined in dodecylphosphocholine micelles using NMR spectroscopy. Dab2 sulfatide-binding motif contains two helices when embedded in micelles, reversibly binds to sulfatides with moderate affinity, lies parallel to the micelle surface, and when added to a platelet mixture, reduces the number and size of sulfatide-induced aggregates. Overall, our findings identify and structurally characterize a minimal region in Dab2 that modulates platelet homotypic interactions, all of which provide the foundation for rational design of a new generation of anti-aggregatory low-molecular mass molecules for therapeutic purposes.","keywords":"Adaptor Proteins, Signal Transducing/*chemistry/genetics/metabolism Amino Acid Motifs Amino Acid Sequence Apoptosis Regulatory Proteins Binding Sites Circular Dichroism Humans Micelles Models, Molecular Molecular Sequence Data Peptides/*chemistry/metabolism/*pharmacology Phosphorylcholine/analogs & derivatives/chemistry Platelet Adhesiveness/drug effects Platelet Aggregation/*drug effects Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Sulfoglycosphingolipids/*chemistry/metabolism Surface Plasmon Resonance Tumor Suppressor Proteins/*chemistry/genetics/metabolism","issn":"0021-9258 (Print) 0021-9258","doi":"10.1074/jbc.M112.385609","year":"2012","bibtex":"@article{RN208,\n author = {Xiao, S. and Charonko, J. J. and Fu, X. and Salmanzadeh, A. and Davalos, R. V. and Vlachos, P. P. and Finkielstein, C. V. and Capelluto, D. G.},\n title = {Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide},\n journal = {J Biol Chem},\n volume = {287},\n number = {45},\n pages = {37691-702},\n note = {1083-351x\nXiao, Shuyan\nCharonko, John J\nFu, Xiangping\nSalmanzadeh, Alireza\nDavalos, Rafael V\nVlachos, Pavlos P\nFinkielstein, Carla V\nCapelluto, Daniel G S\nJournal Article\nResearch Support, Non-U.S. Gov't\nUnited States\n2012/09/15\nJ Biol Chem. 2012 Nov 2;287(45):37691-702. doi: 10.1074/jbc.M112.385609. Epub 2012 Sep 13.},\n abstract = {Disabled-2 (Dab2) targets membranes and triggers a wide range of biological events, including endocytosis and platelet aggregation. Dab2, through its phosphotyrosine-binding (PTB) domain, inhibits platelet aggregation by competing with fibrinogen for α(IIb)β(3) integrin receptor binding. We have recently shown that the N-terminal region, including the PTB domain (N-PTB), drives Dab2 to the platelet membrane surface by binding to sulfatides through two sulfatide-binding motifs, modulating the extent of platelet aggregation. The three-dimensional structure of a Dab2-derived peptide encompassing the sulfatide-binding motifs has been determined in dodecylphosphocholine micelles using NMR spectroscopy. Dab2 sulfatide-binding motif contains two helices when embedded in micelles, reversibly binds to sulfatides with moderate affinity, lies parallel to the micelle surface, and when added to a platelet mixture, reduces the number and size of sulfatide-induced aggregates. Overall, our findings identify and structurally characterize a minimal region in Dab2 that modulates platelet homotypic interactions, all of which provide the foundation for rational design of a new generation of anti-aggregatory low-molecular mass molecules for therapeutic purposes.},\n keywords = {Adaptor Proteins, Signal Transducing/*chemistry/genetics/metabolism\nAmino Acid Motifs\nAmino Acid Sequence\nApoptosis Regulatory Proteins\nBinding Sites\nCircular Dichroism\nHumans\nMicelles\nModels, Molecular\nMolecular Sequence Data\nPeptides/*chemistry/metabolism/*pharmacology\nPhosphorylcholine/analogs & derivatives/chemistry\nPlatelet Adhesiveness/drug effects\nPlatelet Aggregation/*drug effects\nProtein Binding\nProtein Structure, Secondary\nProtein Structure, Tertiary\nSequence Homology, Amino Acid\nSulfoglycosphingolipids/*chemistry/metabolism\nSurface Plasmon Resonance\nTumor Suppressor Proteins/*chemistry/genetics/metabolism},\n ISSN = {0021-9258 (Print)\n0021-9258},\n DOI = {10.1074/jbc.M112.385609},\n year = {2012},\n type = {Journal Article}\n}\n\n","author_short":["Xiao, S.","Charonko, J. 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