Solution Structure of the Apocalmodulin/neuro-P Complex
Short, James Howard
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https://hdl.handle.net/2142/84899
Description
Title
Solution Structure of the Apocalmodulin/neuro-P Complex
Author(s)
Short, James Howard
Issue Date
1998
Doctoral Committee Chair(s)
Wand, A. Joshua
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
The interaction of apocalmodulin with a peptide (Neurop ) derived from the calmodulin-binding domain of the neural-specific protein neuromodulin has been studied by nuclear magnetic resonance (NMR). This complex is in fast exchange with its components on the NMR timescale, and the dissociation constant for the complex is in the micromolar range. This thesis presents the solution structure of the apoCaM. Neurop complex. The 1H, 13C, and 15N resonance assignments for the calmodulin and Neurop components of the complex were determined using multidimensional, multinuclear and triple resonance NMR methods. NOE-derived distance restraints and angular restraints were likewise determined. A total of 1910 intraprotein, 108 intrapeptide, and 18 protein-peptide NOEs were used to generate a family of structures. In addition, 217 torsional restraints and 68 hydrogen bond restraints were used to refine the final generated structures. A family of 48 refined structures was chosen for analysis on the basis of lowest energy and violations. The atomic r. m. s. d. for this family was 1.3 A for main chain atoms and 1.78 A for all heavy atoms. The average structure differs from other known calmodulin-peptide structures in possessing protein domains in which the hydrophobic surfaces normally involved in protein-peptide interactions are either not present (N-terminal domain) or are reduced in size (C-terminal domain). The result is a complex in which the peptide is loosely held by a pair of salt links, one to each domain of the protein, and hydrophobic interactions with the C-terminal domain.
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