NMR studies of human annexin I and yeast guanylate kinase.

摘要

Annexins are excellent models for studying the folding mechanisms of multidomain proteins because they have 4-8 domains with high similarity in folding but low identity in sequence. The solution structure of an isolated domain 1 of human annexin I has been determined by NMR spectroscopy. The root-mean-square deviation of the ensemble of 20 refined conformers was 0.57 ;Guanylate kinase (GK) is a suitable model enzyme for NMR studies of structural and dynamic properties of nucleoside monophosphate kinases. A series of 2D and 3D NMR data have been collected for free and GMP-bound forms of GK. Sequential backbone resonance assignments for the GK complex with GMP have been made. The results obtained in this work provide the basis for the NMR studies of the structure-function relationships of GK. Proposals for the further efforts towards elucidating dynamic and structural changes that control kinase catalysis were also discussed.