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1pbw
From Proteopedia
(New page: 200px<br /> <applet load="1pbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pbw, resolution 2.0Å" /> '''STRUCTURE OF BCR-HOM...) |
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| - | [[Image:1pbw.gif|left|200px]]<br /> | + | [[Image:1pbw.gif|left|200px]]<br /><applet load="1pbw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pbw" size=" | + | |
caption="1pbw, resolution 2.0Å" /> | caption="1pbw, resolution 2.0Å" /> | ||
'''STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN'''<br /> | '''STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proteins such as the product of the break-point cluster region, chimaerin, and the Src homology 3-binding protein 3BP1, are GTPase activating | + | Proteins such as the product of the break-point cluster region, chimaerin, and the Src homology 3-binding protein 3BP1, are GTPase activating proteins (GAPs) for members of the Rho subfamily of small GTP-binding proteins (G proteins or GTPases). A 200-residue region, named the breakpoint cluster region-homology (BH) domain, is responsible for the GAP activity. We describe here the crystal structure of the BH domain from the p85 subunit of phosphatidylinositol 3-kinase at 2.0 A resolution. The domain is composed of seven helices, having a previously unobserved arrangement. A core of four helices contains most residues that are conserved in the BH family. Their packing suggests the location of a G-protein binding site. This structure of a GAP-like domain for small GTP-binding proteins provides a framework for analyzing the function of this class of molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1PBW 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:// | + | 1PBW 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=1PBW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cantley, L | + | [[Category: Cantley, L C.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Musacchio, A.]] | [[Category: Musacchio, A.]] | ||
[[Category: cdc42]] | [[Category: cdc42]] | ||
| Line 26: | Line 25: | ||
[[Category: tpase activating protein]] | [[Category: tpase activating protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:13 2008'' |
Revision as of 12:27, 21 February 2008
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STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN
Overview
Proteins such as the product of the break-point cluster region, chimaerin, and the Src homology 3-binding protein 3BP1, are GTPase activating proteins (GAPs) for members of the Rho subfamily of small GTP-binding proteins (G proteins or GTPases). A 200-residue region, named the breakpoint cluster region-homology (BH) domain, is responsible for the GAP activity. We describe here the crystal structure of the BH domain from the p85 subunit of phosphatidylinositol 3-kinase at 2.0 A resolution. The domain is composed of seven helices, having a previously unobserved arrangement. A core of four helices contains most residues that are conserved in the BH family. Their packing suggests the location of a G-protein binding site. This structure of a GAP-like domain for small GTP-binding proteins provides a framework for analyzing the function of this class of molecules.
About this Structure
1PBW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit., Musacchio A, Cantley LC, Harrison SC, Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14373-8. PMID:8962058
Page seeded by OCA on Thu Feb 21 14:27:13 2008
