2lyp | pdb_00002lyp

NOE-based 3D structure of the monomer of CylR2 in equilibrium with predissociated homodimer at 266K (-7 Celsius degrees)

spinqualitylabelsall models 2lyp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lyp is a 1 chain structure with sequence from Enterococcus faecalis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8VL32_ENTFL Publication Abstract from PubMed Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 degrees C to -16 degrees C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding. Cold denaturation of a protein dimer monitored at atomic resolution.,Jaremko M, Jaremko L, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M Nat Chem Biol. 2013 Feb 10. doi: 10.1038/nchembio.1181. PMID:23396077 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA