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2esw
From Proteopedia
(New page: 200px<br /><applet load="2esw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2esw, resolution 2.01Å" /> '''Atomic structure of ...) |
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| - | [[Image:2esw.gif|left|200px]]<br /><applet load="2esw" size=" | + | [[Image:2esw.gif|left|200px]]<br /><applet load="2esw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2esw, resolution 2.01Å" /> | caption="2esw, resolution 2.01Å" /> | ||
'''Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor'''<br /> | '''Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase | + | The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3(2)21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact beta-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse betaPIX-SH3 domain binding the way in which the betaPIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse betaPIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse betaPIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of betaPIX-SH3 domain resulting in its multiple biological functions. |
==About this Structure== | ==About this Structure== | ||
| - | 2ESW 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 HG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2ESW 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=HG:'>HG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:22 2008'' |
Revision as of 15:14, 21 February 2008
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Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor
Overview
The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3(2)21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact beta-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse betaPIX-SH3 domain binding the way in which the betaPIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse betaPIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse betaPIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of betaPIX-SH3 domain resulting in its multiple biological functions.
About this Structure
2ESW is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor., Li X, Liu X, Sun F, Gao J, Zhou H, Gao GF, Bartlam M, Rao Z, Biochem Biophys Res Commun. 2006 Jan 6;339(1):407-14. Epub 2005 Nov 14. PMID:16307729
Page seeded by OCA on Thu Feb 21 17:14:22 2008
Categories: Mus musculus | Single protein | Rao, Z. | CL | HG | Beta barrel | Sh3 domain
