Summary for 2MY7
Entry DOI | 10.2210/pdb2my7/pdb |
Related | 2MY8 |
NMR Information | BMRB: 19685 |
Descriptor | CUGBP Elav-like family member 2 (1 entity in total) |
Functional Keywords | etr 3 rrm-3, intermediate state, protein folding, rna binding protein |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 10930.56 |
Authors | Bhatt, H.P.,Ganguly, A.K.,Bhavesh, N.S. (deposition date: 2015-01-21, release date: 2015-02-04, Last modification date: 2024-05-15) |
Primary citation | Bhatt, H.,Ganguly, A.K.,Sharma, S.,Kushwaha, G.S.,Firoz Khan, M.,Sen, S.,Bhavesh, N.S. Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold. Biophys.J., 118:352-365, 2020 Cited by PubMed Abstract: Prevalence of one or more partially folded intermediates during protein unfolding with different secondary and ternary conformations has been identified as an integral character of protein unfolding. These transition-state species need to be characterized structurally for elucidation of their folding pathways. We have determined the three-dimensional structure of an intermediate state with increased conformational space sampling under urea-denaturing condition. The protein unfolds completely at 10 M urea but retains residual secondary structural propensities with restricted motion. Here, we describe the native state, observable intermediate state, and unfolded state for ETR-3 RRM-3, which has canonical RRM fold. These observations can shed more light on unfolding events for RRM-containing proteins. PubMed: 31866002DOI: 10.1016/j.bpj.2019.11.3392 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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