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New page: left|200px<br /> <applet load="1by1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by1" /> '''DBL homology domain from beta-PIX'''<br /> ...
 
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[[Image:1by1.gif|left|200px]]<br />
[[Image:1by1.gif|left|200px]]<br /><applet load="1by1" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1by1" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1by1" />
caption="1by1" />
'''DBL homology domain from beta-PIX'''<br />
'''DBL homology domain from beta-PIX'''<br />


==Overview==
==Overview==
Guanine nucleotide exchange factors in the Dbl family activate Rho GTPases, by accelerating dissociation of bound GDP, promoting acquisition of the, GTP-bound state. Dbl proteins possess a approximately 200 residue, catalytic Dbl-homology (DH) domain, that is arranged in tandem with a, C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we, report the solution structure of the DH domain of human PAK-interacting, exchange protein (betaPIX). The domain is composed of 11 alpha-helices, that form a flattened, elongated bundle. The structure explains a large, body of mutagenesis data, which, along with sequence comparisons, identify, the GTPase interaction site as a surface formed by three conserved helices, near the center of one face of the domain. Proximity of the site to the DH, C-terminus suggests a means by which PH-ligand interactions may be coupled, to DH-GTPase interactions to regulate signaling through the Dbl proteins, in vivo.
Guanine nucleotide exchange factors in the Dbl family activate Rho GTPases by accelerating dissociation of bound GDP, promoting acquisition of the GTP-bound state. Dbl proteins possess a approximately 200 residue catalytic Dbl-homology (DH) domain, that is arranged in tandem with a C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we report the solution structure of the DH domain of human PAK-interacting exchange protein (betaPIX). The domain is composed of 11 alpha-helices that form a flattened, elongated bundle. The structure explains a large body of mutagenesis data, which, along with sequence comparisons, identify the GTPase interaction site as a surface formed by three conserved helices near the center of one face of the domain. Proximity of the site to the DH C-terminus suggests a means by which PH-ligand interactions may be coupled to DH-GTPase interactions to regulate signaling through the Dbl proteins in vivo.


==About this Structure==
==About this Structure==
1BY1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BY1 OCA].  
1BY1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY1 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Aghazadeh, B.]]
[[Category: Aghazadeh, B.]]
[[Category: Kubiseski, T.J.]]
[[Category: Kubiseski, T J.]]
[[Category: Liu, G.A.]]
[[Category: Liu, G A.]]
[[Category: Pawson, T.]]
[[Category: Pawson, T.]]
[[Category: Rosen, M.K.]]
[[Category: Rosen, M K.]]
[[Category: Zheng, Y.]]
[[Category: Zheng, Y.]]
[[Category: Zhu, K.]]
[[Category: Zhu, K.]]
[[Category: rho-gtpase exchange factor]]
[[Category: rho-gtpase exchange factor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:23 2008''