2qkd: Difference between revisions

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==Overview==

Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1, domains. In response to growth stimuli, ZPR1 assembles into complexes with, eukaryotic translation elongation factor 1A (eEF1A) and the survival motor, neurons protein. To gain insight into the structural mechanisms underlying, the essential function of ZPR1 in diverse organisms, we determined the, crystal structure of a ZPR1 domain tandem and characterized the, interaction with eEF1A. The ZPR1 domain consists of an elongation, initiation factor 2-like zinc finger and a double-stranded beta helix with, a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A, but does not directly influence the kinetics of nucleotide exchange or GTP, hydrolysis. However, ZPR1 efficiently displaces the exchange factor, eEF1Balpha from preformed nucleotide-free complexes, suggesting that it, may function as a negative regulator of eEF1A activation. Structure-based, mutational and complementation analyses reveal a conserved binding epitope, for eEF1A that is required for normal cell growth, proliferation, and cell, cycle progression. Structural differences between the ZPR1 domains, contribute to the observed functional divergence and provide evidence for, distinct modalities of interaction with eEF1A and survival motor neuron, complexes.

Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.

==About this Structure==

2QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Residue A 501'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Residue A 502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt Binding Site For Residue A 778'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].

2QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Mishra, A.K.]]

[[Category: Mishra, A K.]]

[[Category: FMT]]

[[Category: ZN]]

Line 24:

[[Category: signaling protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1, domains. In response to growth stimuli, ZPR1 assembles into complexes with, eukaryotic translation elongation factor 1A (eEF1A) and the survival motor, neurons protein. To gain insight into the structural mechanisms underlying, the essential function of ZPR1 in diverse organisms, we determined the, crystal structure of a ZPR1 domain tandem and characterized the, interaction with eEF1A. The ZPR1 domain consists of an elongation, initiation factor 2-like zinc finger and a double-stranded beta helix with, a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A, but does not directly influence the kinetics of nucleotide exchange or GTP, hydrolysis. However, ZPR1 efficiently displaces the exchange factor, eEF1Balpha from preformed nucleotide-free complexes, suggesting that it, may function as a negative regulator of eEF1A activation. Structure-based, mutational and complementation analyses reveal a conserved binding epitope, for eEF1A that is required for normal cell growth, proliferation, and cell, cycle progression. Structural differences between the ZPR1 domains, contribute to the observed functional divergence and provide evidence for, distinct modalities of interaction with eEF1A and survival motor neuron, complexes.
+Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.
 ==About this Structure==
-QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Residue A 501'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Residue A 502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt Binding Site For Residue A 778'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].
+QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+501'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+502'>AC2</scene> and <scene name='pdbsite=AC3:Fmt+Binding+Site+For+Residue+A+778'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKD OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Mishra, A.K.]]
+[[Category: Mishra, A K.]]
 [[Category: FMT]]
 [[Category: ZN]]
@@ Line 24: / Line 24: @@
 [[Category: signaling protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:58:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:00 2008''