Literature DB >> 9862438

Obtaining and characterization of EF-hand mutants of recoverin.

A M Alekseev1, S V Shulga-Morskoy, D V Zinchenko, S A Shulga-Morskaya, D V Suchkov, S A Vaganova, I I Senin, A A Zargarov, V M Lipkin, M Akhtar, P P Philippov.   

Abstract

Several EF-hand recoverin mutants were obtained and their abilities to bind to photoreceptor membranes and to inhibit rhodopsin kinase were determined. The mutants with the 'spoiled' 2nd, 3rd or (2nd+3rd) EF-hand structures did not act upon the kinase activity in the microM range of Ca2+ concentrations. Mutations of the 4th EF hand, which 'repaired' its Ca2+-binding activity, resulted in recoverin with three 'working' Ca2+-binding sites. The latter mutant inhibited rhodopsin kinase even more effectively than the wild-type recoverin, containing two working Ca2+-binding structures.

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Year:  1998        PMID: 9862438     DOI: 10.1016/s0014-5793(98)01426-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1).

Authors:  Congmin Li; Wensheng Pan; Karl H Braunewell; James B Ames
Journal:  J Biol Chem       Date:  2010-12-17       Impact factor: 5.157

2.  Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF Hands.

Authors:  Ramasamy P Kumar; Matthew J Ranaghan; Allen Y Ganjei; Daniel D Oprian
Journal:  Biochemistry       Date:  2015-12-03       Impact factor: 3.162

  2 in total

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