2KZG
A Transient and Low Populated Protein Folding Intermediate at Atomic Resolution
Summary for 2KZG
| Entry DOI | 10.2210/pdb2kzg/pdb |
| Related | 1UZC |
| Descriptor | Pre-mRNA-processing factor 40 homolog A (1 entity in total) |
| Functional Keywords | folding intermediate, low populated, relaxation dispersion, cpmg, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus speckle (By similarity): O75400 |
| Total number of polymer chains | 1 |
| Total formula weight | 8251.47 |
| Authors | Korzhnev, D.M.,Religa, T.L.,Banachewicz, W.,Fersht, A.R.,Kay, L.E. (deposition date: 2010-06-17, release date: 2010-09-29, Last modification date: 2024-05-01) |
| Primary citation | Korzhnev, D.M.,Religa, T.L.,Banachewicz, W.,Fersht, A.R.,Kay, L.E. A transient and low-populated protein-folding intermediate at atomic resolution. Science, 329:1312-1316, 2010 Cited by PubMed Abstract: Proteins can sample conformational states that are critical for function but are seldom detected directly because of their low occupancies and short lifetimes. In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, in concert with a chemical shift-based method for structure elucidation, to determine an atomic-resolution structure of an "invisible" folding intermediate of a small protein module: the FF domain. The structure reveals non-native elements preventing formation of the native conformation in the carboxyl-terminal part of the protein. This is consistent with the kinetics of folding in which a well-structured intermediate forms rapidly and then rearranges slowly to the native state. The approach introduces a general strategy for structure determination of low-populated and transiently formed protein states. PubMed: 20829478DOI: 10.1126/science.1191723 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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