Document Detail


Structural differences in the two calcium binding sites of the porcine intestinal calcium binding protein: a multinuclear NMR study.
MedLine Citation:
PMID:  4052373     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cadmium-113 and calcium-43 NMR spectra of Cd2+ and Ca2+ bound to the porcine intestinal calcium binding protein (ICaBP; Mr 9000) contain two resonances. The first resonance is characterized by NMR parameters resembling those found for these cations bound to proteins containing the typical helix-loop-helix calcium binding domains of parvalbumin, calmodulin, and troponin C, which are defined as EF-hands by Kretsinger [Kretsinger, R. H. (1976) Annu. Rev. Biochem. 45, 239]. The second resonance in both spectra has a unique chemical shift and is consequently assigned to the metal ion bound in the N-terminal site of ICaBP. This site is characterized by an insertion of a proline in the loop of the helix-loop-helix domain and will be called the pseudo-EF-hand site. The binding of Cd2+ to the apo form of ICaBP is sequential. The EF-hand site is filled first. Both binding sites have similar, but not identical, affinities for Ca2+: at a Ca2+ to protein ratio of 1:1, 65% of the ion is bound in the EF-hand site and 35% in the pseudo-EF-hand site. The two sites do not appear to act independently; thus, replacement of Ca2+ or Cd2+ by La3+ in the EF-hand site causes changes in the environment of the ions in the pseudo-EF-hand site. In addition, the chemical shift of Cd2+ bound to the EF-hand site is dependent on the presence or absence of Ca2+ or Cd2+ in the pseudo-EF-hand site.(ABSTRACT TRUNCATED AT 250 WORDS)
Authors:
H J Vogel; T Drakenberg; S Forsén; J D O'Neil; T Hofmann
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  24     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1985 Jul 
Date Detail:
Created Date:  1985-12-05     Completed Date:  1985-12-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3870-6     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Calcium / metabolism*
Calcium-Binding Proteins / metabolism*
Cations, Divalent
Duodenum / metabolism*
Ileum / metabolism*
Intestinal Mucosa / metabolism*
Magnetic Resonance Spectroscopy / methods
Protein Binding
Protein Conformation
Swine
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/Cations, Divalent; 7440-70-2/Calcium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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