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000055440 0247_ $$2DOI$$a10.1016/j.jmb.2006.11.013
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000055440 084__ $$2WoS$$aBiochemistry & Molecular Biology
000055440 1001_ $$0P:(DE-Juel1)VDB2063$$aSchmidt, H.$$b0$$uFZJ
000055440 245__ $$aSolution structure of a Hck SH3 domain ligand complex reveals novel interaction modes
000055440 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2007
000055440 300__ $$a1517 - 1532
000055440 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000055440 3367_ $$2BibTeX$$aARTICLE
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000055440 3367_ $$2DRIVER$$aarticle
000055440 440_0 $$03552$$aJournal of Molecular Biology$$v365$$x0022-2836
000055440 500__ $$aRecord converted from VDB: 12.11.2012
000055440 520__ $$aWe studied the interaction of hematopoietic cell kinase SH3 domain (HckSH3) with an artificial 12-residue proline-rich peptide PD1 (HSKYPLPPLPSL) identified as high affinity ligand (K(D)=0.2 muM). PD1 shows an unusual ligand sequence for SH3 binding in type I orientation because it lacks the typical basic anchor residue at position P(-3), but instead has a tyrosine residue at this position. A basic lysine residue, however, is present at position P(-4). The solution structure of the HckSH3:PD1 complex, which is the first HckSH3 complex structure available, clearly reveals that the P(-3) tyrosine residue of PD1 does not take the position of the typical anchor residue but rather forms additional van der Waals interactions with the HckSH3 RT loop. Instead, lysine at position P(-4) of PD1 substitutes the function of the P(-3) anchor residue. This finding expands the well known ligand consensus sequence +xxPpxP by +xxxPpxP. Thus, software tools like iSPOT fail to identify PD1 as a high-affinity HckSH3 ligand so far. In addition, a short antiparallel beta-sheet in the RT loop of HckSH3 is observed upon PD1 binding. The structure of the HckSH3:PD1 complex reveals novel features of SH3 ligand binding and yields new insights into the structural basics of SH3-ligand interactions. Consequences for computational prediction tools adressing SH3-ligand interactions as well as the biological relevance of our findings are discussed.
000055440 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000055440 588__ $$aDataset connected to Web of Science, Pubmed
000055440 650_2 $$2MeSH$$aAmides
000055440 650_2 $$2MeSH$$aAmino Acid Sequence
000055440 650_2 $$2MeSH$$aBinding Sites
000055440 650_2 $$2MeSH$$aDeuterium Oxide: metabolism
000055440 650_2 $$2MeSH$$aHalf-Life
000055440 650_2 $$2MeSH$$aHumans
000055440 650_2 $$2MeSH$$aKinetics
000055440 650_2 $$2MeSH$$aLigands
000055440 650_2 $$2MeSH$$aModels, Molecular
000055440 650_2 $$2MeSH$$aMolecular Sequence Data
000055440 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000055440 650_2 $$2MeSH$$aPeptide Mapping
000055440 650_2 $$2MeSH$$aPeptides: chemistry
000055440 650_2 $$2MeSH$$aPeptides: metabolism
000055440 650_2 $$2MeSH$$aProtein Binding
000055440 650_2 $$2MeSH$$aProto-Oncogene Proteins c-hck: analysis
000055440 650_2 $$2MeSH$$aProto-Oncogene Proteins c-hck: chemistry
000055440 650_2 $$2MeSH$$aProto-Oncogene Proteins c-hck: metabolism
000055440 650_2 $$2MeSH$$aProtons
000055440 650_2 $$2MeSH$$aSolutions
000055440 650_2 $$2MeSH$$aWater: metabolism
000055440 650_2 $$2MeSH$$asrc Homology Domains
000055440 650_7 $$00$$2NLM Chemicals$$aAmides
000055440 650_7 $$00$$2NLM Chemicals$$aLigands
000055440 650_7 $$00$$2NLM Chemicals$$aPeptides
000055440 650_7 $$00$$2NLM Chemicals$$aProtons
000055440 650_7 $$00$$2NLM Chemicals$$aSolutions
000055440 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
000055440 650_7 $$07789-20-0$$2NLM Chemicals$$aDeuterium Oxide
000055440 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aHCK protein, human
000055440 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aProto-Oncogene Proteins c-hck
000055440 650_7 $$2WoSType$$aJ
000055440 65320 $$2Author$$ahuman Hck
000055440 65320 $$2Author$$aSH3-ligand interaction
000055440 65320 $$2Author$$aNMR
000055440 65320 $$2Author$$acomplex structure
000055440 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b1$$uFZJ
000055440 7001_ $$0P:(DE-HGF)0$$aTran, T.$$b2
000055440 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b3$$uFZJ
000055440 7001_ $$0P:(DE-Juel1)VDB8627$$aStangler, T.$$b4$$uFZJ
000055440 7001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b5$$uFZJ
000055440 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b6$$uFZJ
000055440 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2006.11.013$$gVol. 365, p. 1517 - 1532$$p1517 - 1532$$q365<1517 - 1532$$tJournal of molecular biology$$v365$$x0022-2836$$y2007
000055440 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2006.11.013
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000055440 9141_ $$y2007
000055440 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000055440 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
000055440 9201_ $$0I:(DE-Juel1)VDB1045$$gJARA$$kJARA-SIM$$lJülich-Aachen Research Alliance - Simulation Sciences$$x1
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