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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<applet load="1g8i" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1g8i, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN FREQUENIN (NEURONAL CALCIUM SENSOR 1)'''<br />
'''CRYSTAL STRUCTURE OF HUMAN FREQUENIN (NEURONAL CALCIUM SENSOR 1)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1G8I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA, CA, 1PE, P6G and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G8I OCA].
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1G8I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=1PE:'>1PE</scene>, <scene name='pdbligand=P6G:'>P6G</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8I OCA].
==Reference==
==Reference==
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[[Category: ef-hand]]
[[Category: ef-hand]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:01:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:15 2008''

Revision as of 10:47, 21 February 2008


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 , , , and 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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