001     49529
005     20200423204259.0
024 7 _ |a pmid:23115339
|2 pmid
024 7 _ |a 10.1074/jbcM505012200
|2 DOI
024 7 _ |a WOS:000234652000022
|2 WOS
024 7 _ |a 2128/2646
|2 Handle
037 _ _ |a PreJuSER-49529
041 _ _ |a ENG
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Batra-Safferling, R.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB58515
245 _ _ |a Glutamic acid-rich proteins of rod photoreceptors are natively unfolded
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2006
300 _ _ |a 1449 - 1460
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
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440 _ 0 |a Journal of Biological Chemistry
|x 0021-9258
|0 3091
|y 3
|v 281
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 7 |a J
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700 1 _ |a Abarca-Heidemann, K.
|b 1
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700 1 _ |a Körschen, H. G.
|b 2
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700 1 _ |a Tziatzios, C.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Stoldt, M.
|b 4
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700 1 _ |a Budyak, I.
|b 5
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|0 P:(DE-Juel1)VDB44596
700 1 _ |a Willbold, D.
|b 6
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700 1 _ |a Schwalbe, H.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Klein-Seetharaman, J.
|b 8
|u FZJ
|0 P:(DE-Juel1)VDB44599
700 1 _ |a Kaupp, U. B.
|b 9
|u FZJ
|0 P:(DE-Juel1)VDB728
773 _ _ |a 10.1074/jbcM505012200
|g Vol. 281, p. 1449 - 1460
|p 1449 - 1460
|q 281<1449 - 1460
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 281
|y 2006
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbcM505012200
|u http://hdl.handle.net/2128/2646
856 4 _ |u https://juser.fz-juelich.de/record/49529/files/77520.pdf
|y OpenAccess
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913 1 _ |k P33
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914 1 _ |y 2006
915 _ _ |0 StatID:(DE-HGF)0010
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920 1 _ |k IBI-1
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|d 31.12.2006
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920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
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