1CNP

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

Summary for 1CNP

• Entry DOI: 10.2210/pdb1cnp/pdb
• Descriptor: CALCYCLIN (RABBIT, APO) (1 entity in total)
• Functional Keywords: ef-hand, calcium-binding protein, s-100 protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Nucleus envelope (By similarity): P30801
• Total number of polymer chains: 2
• Total formula weight: 20335.46

Authors

Potts, B.C.M.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J. (deposition date: 1995-08-31, release date: 1996-10-14, Last modification date: 2024-05-22)

Primary citation

Potts, B.C.,Smith, J.,Akke, M.,Macke, T.J.,Okazaki, K.,Hidaka, H.,Case, D.A.,Chazin, W.J.
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
Nat.Struct.Biol., 2:790-796, 1995

PubMed Abstract: The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.

PubMed: 7552751
DOI: 10.1038/nsb0995-790

Experimental method

SOLUTION NMR