1CDL

TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX

Summary for 1CDL

• Entry DOI: 10.2210/pdb1cdl/pdb
• Descriptor: CALMODULIN, CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II ALPHA CHAIN, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, spindle: P62158; Cytoplasm, cytosol: P11799
• Total number of polymer chains: 8
• Total formula weight: 76152.64

Authors

Meador, W.E.,Quiocho, F.A. (deposition date: 1993-10-08, release date: 1994-08-31, Last modification date: 2024-02-07)

Primary citation

Meador, W.E.,Means, A.R.,Quiocho, F.A.
Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.
Science, 257:1251-1255, 1992

PubMed Abstract: The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total.

PubMed: 1519061

Experimental method

X-RAY DIFFRACTION (2 Å)