1bo9 Citations

NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit.

J. Biol. Chem. 274 2971-7 (1999)
Cited: 8 times
EuropePMC logo PMID: 9915835

Abstract

Annexins are excellent models for studying the folding mechanisms of multidomain proteins because they have four-eight homologous helical domains with low identity in sequence but high similarity in folding. The structure of an isolated domain 1 of human annexin I has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances of the isolated domain 1 were established by multinuclear, multidimensional NMR spectroscopy. The solution structure of the isolated domain 1 was derived from 1,099 experimental NMR restraints using a hybrid distance geometry-simulated annealing protocol. The root mean square deviation of the ensemble of 20 refined conformers that represent the structure from the mean coordinate set derived from them was 0. 57 +/- 0.14 A and 1.11 +/- 0.19 A for the backbone atoms and all heavy atoms, respectively. The NMR structure of the isolated domain 1 could be superimposed with a root mean square deviation of 1.36 A for all backbone atoms with the corresponding part of the crystal structure of a truncated human annexin I containing all four domains, indicating that the structure of the isolated domain 1 is highly similar to that when it folded together with the other three domains. The result suggests that in contrast to isolated domain 2, which is largely unfolded in solution, isolated domain 1 constitutes an autonomous folding unit and interdomain interactions may play critical roles in the folding of annexin I.

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  1. Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis. Singh SK, Thirumalai A, Hammond DJ, Pangburn MK, Mishra VK, Johnson DA, Rusiñol AE, Agrawal A. J. Biol. Chem. 287 3550-3558 (2012)
  2. Structure prediction for the helical skeletons detected from the low resolution protein density map. Al Nasr K, Sun W, He J. BMC Bioinformatics 11 Suppl 1 S44 (2010)


Reviews citing this publication (1)

  1. Structural studies on rhodopsin. Albert AD, Yeagle PL. Biochim. Biophys. Acta 1565 183-195 (2002)

Articles citing this publication (5)

  1. Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Katragadda M, Alderfer JL, Yeagle PL. Biophys. J. 81 1029-1036 (2001)
  2. High resolution NMR analysis of the seven transmembrane domains of a heptahelical receptor in organic-aqueous medium. Arshava B, Taran I, Xie H, Becker JM, Naider F. Biopolymers 64 161-176 (2002)
  3. Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. Yoon MK, Park SH, Won HS, Na DS, Lee BJ. FEBS Lett. 484 241-245 (2000)
  4. Detecting local structural similarity in proteins by maximizing number of equivalent residues. Standley DM, Toh H, Nakamura H. Proteins 57 381-391 (2004)
  5. Engineering, biophysical characterisation and binding properties of a soluble mutant form of annexin A2 domain IV that adopts a partially folded conformation. Aukrust I, Evensen L, Hollås H, Berven F, Atkinson RA, Travé G, Flatmark T, Vedeler A. J. Mol. Biol. 363 469-481 (2006)