Motion in Calbindin [calbind]

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Classification Known Fragment Motion, Shear Mechanism [F-s-2]

Structures 1CDN Conformation 3 [ PartsList ] 1CLB Conformation 1 [ PartsList ] 4ICB Conformation 2 [ PartsList ]

Description The structure of calbindin is characteristic of an EF-hand protein, with two helix-loop-helix calcium binding motifs joined by a flexible linker, and a short anti-parallel beta-type interaction between the two ion-binding sites. The structure of calbindin has been solved in the apo (Conformation 1), (Ca2+)(2) (Conformation 2), and (Cd2+)(1) (Conformation 3) states in x-ray and NMR studies. Upon binding of both Calcium ions to the structure, the two ion-binding loops in the structure move approximately 1.00 A together, while the pairs of helices in the structure move approximately 0.45 A together.

Particular values describing motion Experimental Methods = xn (Traditional x-ray) Creation Date = 19971130 Modification Date = 19971130

References Z Jia, D Barford, A J Flint, and N K Tonks (1995). Structural Basis for Phosphotyrosine Peptide Recognition by Protein Tyrosine Phosphatase 1B. Sci. 268:1754-1758. [Medline info for 10074413]

GO terms associated with structures Molecular function calcium ion binding

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu