Letter to the Editor: 1H, 15N and 13C resonance assignments of rabbit apo-S100A11

S100 proteins belong to the EF-hand family of calcium binding proteins. Upon calcium binding, these proteins undergo a conformational change to expose a hydrophobic region necessary for target protein interaction. One member of the S100 protein family is S100A11, first isolated from chicken gizzard and termed calgizzarin. It was later isolated from other organisms and tissues including human placenta, pig heart and rabbit lung. The physiological target of S100A11 is thought to be annexin I, a phospholipid-binding protein involved in EGF receptor sorting. This work reports the ¹H, ¹⁵N and ¹³C resonance assignments of rabbit apo-S100A11 determined using ¹⁵N, ¹³C-labelled protein and multidimensional NMR spectroscopy.     

1H, 13C and 15N resonance assignment of Urm1 from Trypanosoma brucei

Urm1 (ubiquitin-related modifier), involved in diverse biological processes in yeast, is proved to be a “molecular fossil” in ubiquitin superfamily. Here we report the resonance assignment of Urm1 from Trypanosoma brucei.