passages.id: split_6_test_2010_passage
passages.type: progene_text
passages.text: Comparison of the structures of the three complexes were useful for identifying the molecular basis of high - affinity : hydrophobic and specific interactions between the side - chains of Y28 and W39 and P5 ' and P4' , respectively , and hydrogen bonds between T37 ( donnor ) and P5' ( acceptor ) and between W39 ( donnor ) and T2' ( acceptor ) stabilize the complex.The structure of the complex L30 K Hu - Yap65 WW domain / GTPPPPYTVG is compared to the published crystal structure of the dystrophin WW domain bound to a segment of the beta-dystroglycan protein and to the solution structure of the first Nedd4 WW domain and its prolin - rich ligand , suggesting that WW sequences bind proline - rich peptides in an evolutionary conserved fashion .