Solution NMR Structure of the Ca²⁺-bound N-terminal Domain of CaBP7 A REGULATOR OF GOLGI TRAFFICKING

McCue, Hannah V, Patel, Pryank, Herbert, Andrew P, Lian, Lu-Yun ORCID: 0000-0001-9481-749X, Burgoyne, Robert D ORCID: 0000-0002-9219-0387 and Haynes, Lee P (2012) Solution NMR Structure of the Ca²⁺-bound N-terminal Domain of CaBP7 A REGULATOR OF GOLGI TRAFFICKING JOURNAL OF BIOLOGICAL CHEMISTRY, 287 (45). pp. 38231-38243. ISSN 0021-9258, 1083-351X

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Abstract

Background: CaBP7 is an EF-hand-containing transmembrane protein that inhibits PI4KIIIβ activity. Results: PI4KIIIβ interacts with CaBP7 NTD, which exhibits an expansive hydrophobic pocket. Conclusion: The structure of CaBP7 NTD is similar to that of CaM NTD but has a more expansive hydrophobic pocket containing fewer methionine residues. Significance: Regulation of PI4P synthesis is essential for vesicle trafficking and secretory pathway function. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

Item Type:	Article
Additional Information:	This research was originally published in Journal of Biological Chemistry. Hannah V. McCue, Pryank Patel, Andrew P. Herbert, Lu-Yun Lian, Robert D. Burgoyne, and Lee P. Haynes. Solution NMR Structure of the Ca2+-Bound N-Terminal Domain of Calcium Binding Protein 7 (CaBP7): A regulator of Golgi trafficking. Journal of Biological Chemistry. 2012; 287: 38231-38243 © the American Society for Biochemistry and Molecular Biology
Uncontrolled Keywords:	Golgi Apparatus, Animals, Cattle, Humans, Calcium, Phosphotransferases (Alcohol Group Acceptor), Calcium-Binding Proteins, Minor Histocompatibility Antigens, Solutions, Blotting, Western, Circular Dichroism, Magnetic Resonance Spectroscopy, Binding Sites, Amino Acid Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Binding, Sequence Homology, Amino Acid, Protein Transport, Surface Properties, Models, Molecular, Molecular Sequence Data, Hydrophobic and Hydrophilic Interactions
Depositing User:	Symplectic Admin
Date Deposited:	24 Apr 2015 14:09
Last Modified:	16 Jun 2026 05:35
DOI:	10.1074/jbc.M112.402289
Related Websites:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/2010467
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