1CMF

NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Calcium-induced structural changes and domain autonomy in calmodulin.

Finn, B.E.Evenas, J.Drakenberg, T.Waltho, J.P.Thulin, E.Forsen, S.

(1995) Nat Struct Biol 2: 777-783

  • DOI: https://doi.org/10.1038/nsb0995-777
  • Primary Citation of Related Structures:  
    1CMF, 1CMG

  • PubMed Abstract: 

    We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.


  • Organizational Affiliation

    Department of Physical Chemistry, Lund University, Sweden.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CALMODULIN (VERTEBRATE)73Bos taurusMutation(s): 0 
UniProt
Find proteins for P62157 (Bos taurus)
Explore P62157 
Go to UniProtKB:  P62157
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UniProt GroupP62157
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-12-07
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations, Other