Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions (364 views) (PDF restricted 188 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2016 Dec 05; 22(49): 17767-17775.
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Paper type: Journal Article,
Impact factor: 5.317, 5-year impact factor: 5.184
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84995393711&doi=10.1002%2fchem.201603650&partnerID=40&md5=4d26bc2f6019fac0f54e0f5dc5e3b397
Keywords: Analytical Methods, Copper, Protein-Protein Interactions, Structural Biology, Structure Elucidation,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via P. Gaifami18, 95126, Catania, Italy., Center for Neural Science, New York University, 4 Washington Pl, New York, NY, 10003, USA., Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Universita di Napoli, Via Vivaldi 43, 81100, Caserta, Italy., Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, V.le A.Doria 6, 95125, Catania, Italy.,
References:
Not available.
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2016 Dec 05; 22(49): 17767-17775.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.317, 5-year impact factor: 5.184
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84995393711&doi=10.1002%2fchem.201603650&partnerID=40&md5=4d26bc2f6019fac0f54e0f5dc5e3b397
Keywords: Analytical Methods, Copper, Protein-Protein Interactions, Structural Biology, Structure Elucidation,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via P. Gaifami18, 95126, Catania, Italy., Center for Neural Science, New York University, 4 Washington Pl, New York, NY, 10003, USA., Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Seconda Universita di Napoli, Via Vivaldi 43, 81100, Caserta, Italy., Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, V.le A.Doria 6, 95125, Catania, Italy.,
References:
Not available.
Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions
Many biochemical pathways involving nerve growth factor (NGF), a neurotrophin with copper(II) binding abilities, are regulated by the ubiquitin (Ub) proteasome system. However, whether NGF binds Ub and the role played by copper(II) ions in modulating their interactions have not yet been investigated. Herein NMR spectroscopy, circular dichroism, ESI-MS, and titration calorimetry are employed to characterize the interactions of NGF with Ub. NGF1-14 , which is a short model peptide encompassing the first 14 N-terminal residues of NGF, binds the copper-binding regions of Ub (KD =8.6 10-5 m). Moreover, the peptide undergoes a random coil-polyproline type II helix structural conversion upon binding to Ub. Notably, copper(II) ions inhibit NGF1-14 /Ub interactions. Further experiments performed with the full-length NGF confirmed the existence of a copper(II)-dependent association between Ub and NGF and indicated that the N-terminal domain of NGF was a valuable paradigm that recapitulated many traits of the full-length protein.
Many biochemical pathways involving nerve growth factor (NGF), a neurotrophin with copper(II) binding abilities, are regulated by the ubiquitin (Ub) proteasome system. However, whether NGF binds Ub and the role played by copper(II) ions in modulating their interactions have not yet been investigated. Herein NMR spectroscopy, circular dichroism, ESI-MS, and titration calorimetry are employed to characterize the interactions of NGF with Ub. NGF1-14 , which is a short model peptide encompassing the first 14 N-terminal residues of NGF, binds the copper-binding regions of Ub (KD =8.6 10-5 m). Moreover, the peptide undergoes a random coil-polyproline type II helix structural conversion upon binding to Ub. Notably, copper(II) ions inhibit NGF1-14 /Ub interactions. Further experiments performed with the full-length NGF confirmed the existence of a copper(II)-dependent association between Ub and NGF and indicated that the N-terminal domain of NGF was a valuable paradigm that recapitulated many traits of the full-length protein.
Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions
Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions
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28 Records (26 excluding Abstracts).
Total impact factor: 90.133 (85.245 excluding Abstracts).
Total 5 year impact factor: 99.138 (93.654 excluding Abstracts).
Total impact factor: 90.133 (85.245 excluding Abstracts).
Total 5 year impact factor: 99.138 (93.654 excluding Abstracts).
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