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000009746 084__ $$2WoS$$aBiochemistry & Molecular Biology
000009746 1001_ $$0P:(DE-Juel1)VDB58515$$aBatra-Safferling, R.$$b0$$uFZJ
000009746 245__ $$aStructural studies of PI3K SH3 domain in complex with a peptide ligand: role of anchor residue in ligand binding
000009746 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2010
000009746 300__ $$a33 - 42
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000009746 440_0 $$09042$$aBiological Chemistry$$v391$$x1431-6730$$y1
000009746 500__ $$aThe authors wish to thank Georg Buldt for continuous generous support. Furthermore, technical assistance by Esther Jonas and the beamline scientists at the ESRF (Grenoble, France) is acknowledged. We also thank Oliver Weiergraber for critical reading of the manuscript. This work was supported by a grant from the Deutsche Forschungsgemeinschaft (SFB 575, B11) to D.W.
000009746 520__ $$aSrc 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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000009746 65320 $$2Author$$aphosphatidylinositol 3-kinase
000009746 65320 $$2Author$$apolyproline helix
000009746 65320 $$2Author$$aprotein-ligand interaction
000009746 65320 $$2Author$$aSrc homology 3
000009746 65320 $$2Author$$api stacking
000009746 650_2 $$2MeSH$$aAmino Acid Sequence
000009746 650_2 $$2MeSH$$aBinding Sites
000009746 650_2 $$2MeSH$$aCrystallography, X-Ray
000009746 650_2 $$2MeSH$$aLigands
000009746 650_2 $$2MeSH$$aModels, Molecular
000009746 650_2 $$2MeSH$$aMolecular Sequence Data
000009746 650_2 $$2MeSH$$aOligopeptides: metabolism
000009746 650_2 $$2MeSH$$aPeptides: chemistry
000009746 650_2 $$2MeSH$$aPhosphatidylinositol 3-Kinases: chemistry
000009746 650_2 $$2MeSH$$aPhosphatidylinositol 3-Kinases: metabolism
000009746 650_2 $$2MeSH$$aProtein Binding
000009746 650_2 $$2MeSH$$asrc Homology Domains: physiology
000009746 650_7 $$00$$2NLM Chemicals$$aLigands
000009746 650_7 $$00$$2NLM Chemicals$$aOligopeptides
000009746 650_7 $$00$$2NLM Chemicals$$aPeptides
000009746 650_7 $$00$$2NLM Chemicals$$ahistidyl-seryl-lysyl-arginyl-prolyl-leucyl-prolyl-prolyl-leucyl-prolyl-seryl-leucine
000009746 650_7 $$025191-13-3$$2NLM Chemicals$$apolyproline
000009746 650_7 $$0EC 2.7.1.-$$2NLM Chemicals$$aPhosphatidylinositol 3-Kinases
000009746 650_7 $$2WoSType$$aJ
000009746 7001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b1$$uFZJ
000009746 7001_ $$0P:(DE-Juel1)VDB92202$$aMoedder, S.$$b2$$uFZJ
000009746 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b3$$uFZJ
000009746 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
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