Home > Publications database > Structural studies of PI3K SH3 domain in complex with a peptide ligand: role of anchor residue in ligand binding > print

001     9746
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024 7 _ |a pmid:19919182
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024 7 _ |a 10.1515/BC.2010.003
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037 _ _ |a PreJuSER-9746
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |0 P:(DE-Juel1)VDB58515
|a Batra-Safferling, R.
|b 0
|u FZJ
245 _ _ |a Structural studies of PI3K SH3 domain in complex with a peptide ligand: role of anchor residue in ligand binding
260 _ _ |a Berlin [u.a.]
|b de Gruyter
|c 2010
300 _ _ |a 33 - 42
336 7 _ |a Journal Article
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336 7 _ |a article
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440 _ 0 |0 9042
|a Biological Chemistry
|v 391
|x 1431-6730
|y 1
500 _ _ |a The authors wish to thank Georg Buldt for continuous generous support. Furthermore, technical assistance by Esther Jonas and the beamline scientists at the ESRF (Grenoble, France) is acknowledged. We also thank Oliver Weiergraber for critical reading of the manuscript. This work was supported by a grant from the Deutsche Forschungsgemeinschaft (SFB 575, B11) to D.W.
520 _ _ |a Src homology 3 (SH3) domains are mediators of protein-protein interactions. They comprise approximately 60 amino acid residues and are found in many intracellular signaling proteins. Here, we present the crystal structure of the SH3 domain from phosphatidylinositol 3-kinase (PI3K) in complex with the 12-residue proline-rich peptide PD1R (HSKRPLPPLPSL). The crystal structure of the PI3K SH3-PD1R complex at a resolution of 1.7 A reveals type I ligand orientation of the bound peptide with an extended conformation where the central portion forms a left-handed type II polyproline (PPII) helix. The overall structure of the SH3 domain shows minimal changes on ligand binding. In addition, we also attempted crystallization with another peptide ligand (PD1) where the residue at anchor position P(-3) is a tyrosine. The crystals obtained did not contain the PD1 ligand; instead, the ligand binding site is partially occupied by residues Arg18 and Trp55 from the symmetry-related PI3K SH3 molecule. Considering these crystal structures of PI3K SH3 together with published reports, we provide a comparative analysis of protein-ligand interactions that has helped us identify the individual residues which play an important role in defining target specificity.
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Ligands
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Oligopeptides: metabolism
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Phosphatidylinositol 3-Kinases: chemistry
650 _ 2 |2 MeSH
|a Phosphatidylinositol 3-Kinases: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a src Homology Domains: physiology
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Oligopeptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a histidyl-seryl-lysyl-arginyl-prolyl-leucyl-prolyl-prolyl-leucyl-prolyl-seryl-leucine
650 _ 7 |0 25191-13-3
|2 NLM Chemicals
|a polyproline
650 _ 7 |0 EC 2.7.1.-
|2 NLM Chemicals
|a Phosphatidylinositol 3-Kinases
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a phosphatidylinositol 3-kinase
653 2 0 |2 Author
|a polyproline helix
653 2 0 |2 Author
|a protein-ligand interaction
653 2 0 |2 Author
|a Src homology 3
653 2 0 |2 Author
|a pi stacking
700 1 _ |0 P:(DE-Juel1)131965
|a Granzin, J.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB92202
|a Moedder, S.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB630
|a Hoffmann, S.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
|b 4
|u FZJ
773 _ _ |0 PERI:(DE-600)1466062-3
|a 10.1515/bc.2010.003
|g Vol. 391, p. 33 - 42
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|v 391
|x 1431-6730
|y 2010
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