1g8i

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(New page: 200px<br /> <applet load="1g8i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g8i, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:55, 12 November 2007


1g8i, resolution 1.90Å

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CRYSTAL STRUCTURE OF HUMAN FREQUENIN (NEURONAL CALCIUM SENSOR 1)

Overview

Frequenin, a member of a large family of myristoyl-switch calcium-binding, proteins, functions as a calcium-ion sensor to modulate synaptic activity, and secretion. We show that human frequenin colocalizes with ARF1 GTPase, in COS-7 cells and occurs in similar cellular compartments as the, phosphatidylinositol-4-OH kinase PI4Kbeta, the mammalian homolog of the, yeast kinase PIK1. In addition, the crystal structure of unmyristoylated, calcium-bound human frequenin has been determined and refined to 1.9 A, resolution. The overall fold of frequenin resembles those of neurocalcin, and the photoreceptor, recoverin, of the same family, with two pairs of, calcium-binding EF hands and three bound calcium ions. Despite the, similarities, however, frequenin displays significant structural, differences. A large conformational shift of the C-terminal region creates, a wide hydrophobic crevice at the surface of frequenin. This crevice, which is unique to frequenin and distinct from the myristoyl-binding box, of recoverin, may accommodate a yet unknown protein ligand.

About this Structure

1G8I is a Single protein structure of sequence from Homo sapiens with NA, CA, 1PE, P6G and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1)., Bourne Y, Dannenberg J, Pollmann V, Marchot P, Pongs O, J Biol Chem. 2001 Apr 13;276(15):11949-55. Epub 2000 Nov 22. PMID:11092894

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