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| Home > Publications database > Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner. > print |
| 001 | 119641 | ||
| 005 | 20240228134946.0 | ||
| 024 | 7 | _ | |a 10.1016/j.bbrc.2013.11.063 |2 doi |
| 024 | 7 | _ | |a pmid:24269589 |2 pmid |
| 024 | 7 | _ | |a 0006-291X |2 ISSN |
| 024 | 7 | _ | |a 1090-2104 |2 ISSN |
| 037 | _ | _ | |a DKFZ-2017-00272 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Berbís, M Álvaro |b 0 |
| 245 | _ | _ | |a Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner. |
| 260 | _ | _ | |a Orlando, Fla. |c 2014 |b Academic Press |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1520586996_4496 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Galectin-3 (Gal-3) is a multi-functional effector protein that functions in the cytoplasm and the nucleus, as well as extracellularly following non-classical secretion. Structurally, Gal-3 is unique among galectins with its carbohydrate recognition domain (CRD) attached to a rather long N-terminal tail composed mostly of collagen-like repeats (nine in the human protein) and terminating in a short non-collagenous terminal peptide sequence unique in this lectin family and not yet fully explored. Although several Ser and Tyr sites within the N-terminal tail can be phosphorylated, the physiological significance of this post-translational modification remains unclear. Here, we used a series of synthetic (phospho)peptides derived from the tail to assess phosphorylation-mediated interactions with (15)N-labeled Gal-3 CRD. HSQC-derived chemical shift perturbations revealed selective interactions at the backface of the CRD that were attenuated by phosphorylation of Tyr 107 and Tyr 118, while phosphorylation of Ser 6 and Ser 12 was essential. Controls with sequence scrambling underscored inherent specificity. Our studies shed light on how phosphorylation of the N-terminal tail may impact on Gal-3 function and prompt further studies using phosphorylated full-length protein. |
| 536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Carbohydrates |2 NLM Chemicals |
| 650 | _ | 7 | |a Galectin 3 |2 NLM Chemicals |
| 650 | _ | 7 | |a Peptides |2 NLM Chemicals |
| 650 | _ | 7 | |a Recombinant Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Tyrosine |0 42HK56048U |2 NLM Chemicals |
| 700 | 1 | _ | |a André, Sabine |b 1 |
| 700 | 1 | _ | |a Cañada, F Javier |b 2 |
| 700 | 1 | _ | |a Pipkorn, Rüdiger |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Ippel, Hans |b 4 |
| 700 | 1 | _ | |a Mayo, Kevin H |b 5 |
| 700 | 1 | _ | |a Kübler, Dieter |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Gabius, Hans-Joachim |b 7 |
| 700 | 1 | _ | |a Jiménez-Barbero, Jesús |b 8 |
| 773 | _ | _ | |a 10.1016/j.bbrc.2013.11.063 |g Vol. 443, no. 1, p. 126 - 131 |0 PERI:(DE-600)1461396-7 |n 1 |p 126 - 131 |t Biochemical and biophysical research communications |v 443 |y 2014 |x 0006-291X |
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| 910 | 1 | _ | |a Deutsches Krebsforschungszentrum |0 I:(DE-588b)2036810-0 |k DKFZ |b 3 |6 P:(DE-HGF)0 |
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