Abstract:
:Here, we present a structural and dynamic description of CBP-ID4 at atomic resolution. ID4 is the fourth intrinsically disordered linker of CREB-binding protein (CBP). In spite of the largely disordered nature of CBP-ID4, NMR chemical shifts and relaxation measurements show a significant degree of α-helix sampling in the protein regions encompassing residues 2-25 and 101-128 (1852-1875 and 1951-1978 in full-length CBP). Proline residues are uniformly distributed along the polypeptide, except for the two α-helical regions, indicating that they play an active role in modulating the structural features of this CBP fragment. The two helical regions are lacking known functional motifs, suggesting that they represent thus-far uncharacterized functional modules of CBP. This work provides insights into the functions of this protein linker that may exploit its plasticity to modulate the relative orientations of neighboring folded domains of CBP and fine-tune its interactions with a multitude of partners.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Piai A,Calçada EO,Tarenzi T,Grande AD,Varadi M,Tompa P,Felli IC,Pierattelli Rdoi
10.1016/j.bpj.2015.11.3516subject
Has Abstractpub_date
2016-01-19 00:00:00pages
372-381issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(15)04700-1journal_volume
110pub_type
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