2esw

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(New page: 200px<br /><applet load="2esw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2esw, resolution 2.01&Aring;" /> '''Atomic structure of ...)
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[[Image:2esw.gif|left|200px]]<br /><applet load="2esw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2esw, resolution 2.01&Aring;" />
caption="2esw, resolution 2.01&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ESW OCA].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:07:30 2007''
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''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

Image:2esw.gif

2esw, resolution 2.01Å

Drag the structure with the mouse to rotate

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

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