1k4u

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(New page: 200px<br /> <applet load="1k4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k4u" /> '''Solution structure of the C-terminal SH3 do...)
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<applet load="1k4u" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox'''<br />
'''Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox'''<br />
==Overview==
==Overview==
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The basic function of the Src homology 3 (SH3) domain is considered to be, binding to proline-rich sequences containing a PxxP motif. Recently, many, SH3 domains, including those from Grb2 and Pex13p, were reported to bind, sequences lacking a PxxP motif. We report here that the 22 residue peptide, lacking a PxxP motif, derived from p47(phox), binds to the C-terminal SH3, domain from p67(phox). We applied the NMR cross-saturation method to, locate the interaction sites for the non-PxxP peptides on their cognate, SH3 domains from p67(phox), Grb2 and Pex13p. The binding site of the Grb2, SH3 partially overlapped the conventional PxxP-binding site, whereas those, of p67(phox) and Pex13p SH3s are located in different surface regions. The, non-PxxP peptide from p47(phox) binds to the p67(phox) SH3 more tightly, when it extends to the N-terminus to include a typical PxxP motif, which, enabled the structure determination of the complex, to reveal that the, non-PxxP peptide segment interacted with the p67(phox) SH3 in a compact, helix-turn-helix structure (PDB entry 1K4U).
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The basic function of the Src homology 3 (SH3) domain is considered to be binding to proline-rich sequences containing a PxxP motif. Recently, many SH3 domains, including those from Grb2 and Pex13p, were reported to bind sequences lacking a PxxP motif. We report here that the 22 residue peptide lacking a PxxP motif, derived from p47(phox), binds to the C-terminal SH3 domain from p67(phox). We applied the NMR cross-saturation method to locate the interaction sites for the non-PxxP peptides on their cognate SH3 domains from p67(phox), Grb2 and Pex13p. The binding site of the Grb2 SH3 partially overlapped the conventional PxxP-binding site, whereas those of p67(phox) and Pex13p SH3s are located in different surface regions. The non-PxxP peptide from p47(phox) binds to the p67(phox) SH3 more tightly when it extends to the N-terminus to include a typical PxxP motif, which enabled the structure determination of the complex, to reveal that the non-PxxP peptide segment interacted with the p67(phox) SH3 in a compact helix-turn-helix structure (PDB entry 1K4U).
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1K4U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1K4U OCA].
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1K4U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1K4U OCA].
==Reference==
==Reference==
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[[Category: sh3-peptide complex]]
[[Category: sh3-peptide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:47:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:09 2008''

Revision as of 11:30, 21 February 2008


1k4u

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Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox

Contents

Overview

The basic function of the Src homology 3 (SH3) domain is considered to be binding to proline-rich sequences containing a PxxP motif. Recently, many SH3 domains, including those from Grb2 and Pex13p, were reported to bind sequences lacking a PxxP motif. We report here that the 22 residue peptide lacking a PxxP motif, derived from p47(phox), binds to the C-terminal SH3 domain from p67(phox). We applied the NMR cross-saturation method to locate the interaction sites for the non-PxxP peptides on their cognate SH3 domains from p67(phox), Grb2 and Pex13p. The binding site of the Grb2 SH3 partially overlapped the conventional PxxP-binding site, whereas those of p67(phox) and Pex13p SH3s are located in different surface regions. The non-PxxP peptide from p47(phox) binds to the p67(phox) SH3 more tightly when it extends to the N-terminus to include a typical PxxP motif, which enabled the structure determination of the complex, to reveal that the non-PxxP peptide segment interacted with the p67(phox) SH3 in a compact helix-turn-helix structure (PDB entry 1K4U).

Disease

Known diseases associated with this structure: Chronic granulomatous disease due to deficiency of NCF-1 OMIM:[608512], Chronic granulomatous disease due to deficiency of NCF-2 OMIM:[608515]

About this Structure

1K4U is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p., Kami K, Takeya R, Sumimoto H, Kohda D, EMBO J. 2002 Aug 15;21(16):4268-76. PMID:12169629

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