1by1
From Proteopedia
(New page: 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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'''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 | + | 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:// | + | 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 | + | [[Category: Kubiseski, T J.]] |
| - | [[Category: Liu, G | + | [[Category: Liu, G A.]] |
[[Category: Pawson, T.]] | [[Category: Pawson, T.]] | ||
| - | [[Category: Rosen, M | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:23 2008'' |
Revision as of 10:00, 21 February 2008
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DBL homology domain from beta-PIX
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.
About this Structure
1BY1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and mutagenesis of the Dbl homology domain., Aghazadeh B, Zhu K, Kubiseski TJ, Liu GA, Pawson T, Zheng Y, Rosen MK, Nat Struct Biol. 1998 Dec;5(12):1098-107. PMID:9846881
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