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@ARTICLE{Schulte:845267,
      author       = {Schulte, Marianne and Panwalkar, Vineet and Freischem,
                      Stefan and Willbold, Dieter and Dingley, Andrew J.},
      title        = {{P}roline {R}estricts {L}oop {I} {C}onformation of the
                      {H}igh {A}ffinity {WW} {D}omain from {H}uman {N}edd4-1 to a
                      {L}igand {B}inding-{C}ompetent {T}ype {I} β-{T}urn},
      journal      = {The journal of physical chemistry / B},
      volume       = {122},
      number       = {15},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-02548},
      pages        = {4219 - 4230},
      year         = {2018},
      abstract     = {Sequence alignment of the four WW domains from human
                      Nedd4-1 (neuronal precursor cell expressed developmentally
                      down-regulated gene 4-1) reveals that the highest sequence
                      diversity exists in loop I. Three residues in this type I
                      β-turn interact with the PPxY motif of the human epithelial
                      Na+ channel (hENaC) subunits, indicating that peptide
                      affinity is defined by the loop I sequence. The third WW
                      domain (WW3*) has the highest ligand affinity and unlike the
                      other three hNedd4-1 WW domains or other WW domains studied
                      contains the highly statistically preferred proline at the
                      (i + 1) position found in β-turns. In this report,
                      molecular dynamics simulations and experimental data were
                      combined to characterize loop I stability and dynamics.
                      Exchange of the proline to the equivalent residue in WW4
                      (Thr) results in the presence of a predominantly open seven
                      residue Ω loop rather than the type I β-turn conformation
                      for the wild-type apo-WW3*. In the presence of the ligand,
                      the structure of the mutated loop I is locked into a type I
                      β-turn. Thus, proline in loop I ensures a stable peptide
                      binding-competent β-turn conformation, indicating that
                      amino acid sequence modulates local flexibility to tune
                      binding preferences and stability of dynamic interaction
                      motifs.},
      cin          = {ICS-6},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29595969},
      UT           = {WOS:000430784000004},
      doi          = {10.1021/acs.jpcb.7b11637},
      url          = {https://juser.fz-juelich.de/record/845267},
}