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@ARTICLE{BatraSafferling:49529,
      author       = {Batra-Safferling, R. and Abarca-Heidemann, K. and
                      Körschen, H. G. and Tziatzios, C. and Stoldt, M. and
                      Budyak, I. and Willbold, D. and Schwalbe, H. and
                      Klein-Seetharaman, J. and Kaupp, U. B.},
      title        = {{G}lutamic acid-rich proteins of rod photoreceptors are
                      natively unfolded},
      journal      = {The journal of biological chemistry},
      volume       = {281},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-49529},
      pages        = {1449 - 1460},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Broadly neutralizing HIV antibodies (bNAbs) can recognize
                      carbohydrate-dependent epitopes on gp120. In contrast to
                      previously characterized glycan-dependent bNAbs that
                      recognize high-mannose N-glycans, PGT121 binds complex-type
                      N-glycans in glycan microarrays. We isolated the B-cell
                      clone encoding PGT121, which segregates into PGT121-like and
                      10-1074-like groups distinguished by sequence, binding
                      affinity, carbohydrate recognition, and neutralizing
                      activity. Group 10-1074 exhibits remarkable potency and
                      breadth but no detectable binding to protein-free glycans.
                      Crystal structures of unliganded PGT121, 10-1074, and their
                      likely germ-line precursor reveal that differential
                      carbohydrate recognition maps to a cleft between
                      complementarity determining region (CDR)H2 and CDRH3. This
                      cleft was occupied by a complex-type N-glycan in a
                      "liganded" PGT121 structure. Swapping glycan contact
                      residues between PGT121 and 10-1074 confirmed their
                      importance for neutralization. Although PGT121 binds
                      complex-type N-glycans, PGT121 recognized high-mannose-only
                      HIV envelopes in isolation and on virions. As HIV envelopes
                      exhibit varying proportions of high-mannose- and
                      complex-type N-glycans, these results suggest promiscuous
                      carbohydrate interactions, an advantageous adaptation
                      ensuring neutralization of all viruses within a given
                      strain.},
      keywords     = {J (WoSType)},
      cin          = {IBI-1 / IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57 / I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23115339},
      UT           = {WOS:000234652000022},
      doi          = {10.1074/jbcM505012200},
      url          = {https://juser.fz-juelich.de/record/49529},
}