1AHR

CALMODULIN MUTANT WITH A TWO RESIDUE DELETION IN THE CENTRAL HELIX

Summary for 1AHR

• Entry DOI: 10.2210/pdb1ahr/pdb
• Descriptor: CALMODULIN, CALCIUM ION (3 entities in total)
• Functional Keywords: calmodulin, calcium-binding protein
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 16638.45

Authors

Tabernero, L.,Sack, J. (deposition date: 1997-04-10, release date: 1997-06-16, Last modification date: 2024-05-22)

Primary citation

Tabernero, L.,Taylor, D.A.,Chandross, R.J.,VanBerkum, M.F.,Means, A.R.,Quiocho, F.A.,Sack, J.S.
The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding.
Structure, 5:613-622, 1997

PubMed Abstract: Calmodulin (CaM) is the major calcium-dependent regulator of a large variety of important intracellular processes in eukaryotes. The structure of CaM consists of two globular calcium-binding domains joined by a central 28-residue alpha helix. This linker helix has been hypothesized to act as a flexible tether and is crucial for the binding and activation of numerous target proteins. Although the way in which alterations of the central helix modulate the molecular recognition mechanism is not known exactly, the relative orientation of the globular domains seems to be of great importance. The structural analysis of central helix mutants may contribute to a better understanding of how changes in the conformation of CaM effect its function.

PubMed: 9195880
DOI: 10.1016/S0969-2126(97)00217-7

Experimental method

X-RAY DIFFRACTION (1.8 Å)