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2MY7

NMR Structure of unfolding intermediate state of RRM-3 domain of ETR-3

Replaces:  2MIK
Summary for 2MY7
Entry DOI10.2210/pdb2my7/pdb
Related2MY8
NMR InformationBMRB: 19685
DescriptorCUGBP Elav-like family member 2 (1 entity in total)
Functional Keywordsetr 3 rrm-3, intermediate state, protein folding, rna binding protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight10930.56
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 citationBhatt, 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: 31866002
DOI: 10.1016/j.bpj.2019.11.3392
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

数据于2024-10-30公开中

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