This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1zsg
From Proteopedia
(New page: 200px<br /> <applet load="1zsg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zsg" /> '''beta PIX-SH3 complexed with an atypical pep...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zsg.gif|left|200px]]<br /> | + | [[Image:1zsg.gif|left|200px]]<br /><applet load="1zsg" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zsg" size=" | + | |
caption="1zsg" /> | caption="1zsg" /> | ||
'''beta PIX-SH3 complexed with an atypical peptide from alpha-PAK'''<br /> | '''beta PIX-SH3 complexed with an atypical peptide from alpha-PAK'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The PAK Ser/Thr kinases are important downstream effectors of the Rho | + | The PAK Ser/Thr kinases are important downstream effectors of the Rho family GTPases Cdc42 and Rac, partly mediating the role of these G proteins in cell proliferation and cytoskeletal rearrangements. As well as small G proteins, PAK interacts with the Cdc42/Rac exchange factor beta-PIX via the PIX SH3 domain and a nontypical Pro-rich region in PAK. This interaction is thought to affect the localization of PAK, as well as increased GTP/GDP exchange of Rac and Cdc42. We have determined the structure of the PIX-SH3/PAK peptide complex and shown that it differs from typical Src-like SH3/peptide complexes. The peptide makes contacts through the Pro-rich sequence in a similar way to standard SH3/peptide complexes, even though the Pro residue positions are not conserved. In addition, there are interactions with a Pro and Lys in the PAK, which are C-terminal to the conserved Arg found in all SH3-binding sequences. These contact a fourth binding pocket on the SH3 domain. We have measured the affinity of PIX-SH3 for the PAK peptide and found that it is of intermediate affinity. When PAK is activated, Ser-199 in the PIX-binding site is phosphorylated. This phosphorylation is sufficient to reduce the affinity for PIX 6-fold. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZSG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http:// | + | 1ZSG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZSG OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Evetts, K | + | [[Category: Evetts, K A.]] |
| - | [[Category: Mott, H | + | [[Category: Mott, H R.]] |
[[Category: Nietlispach, D.]] | [[Category: Nietlispach, D.]] | ||
[[Category: Owen, D.]] | [[Category: Owen, D.]] | ||
[[Category: sh3-peptide complex]] | [[Category: sh3-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:43 2008'' |
Revision as of 14:18, 21 February 2008
|
beta PIX-SH3 complexed with an atypical peptide from alpha-PAK
Overview
The PAK Ser/Thr kinases are important downstream effectors of the Rho family GTPases Cdc42 and Rac, partly mediating the role of these G proteins in cell proliferation and cytoskeletal rearrangements. As well as small G proteins, PAK interacts with the Cdc42/Rac exchange factor beta-PIX via the PIX SH3 domain and a nontypical Pro-rich region in PAK. This interaction is thought to affect the localization of PAK, as well as increased GTP/GDP exchange of Rac and Cdc42. We have determined the structure of the PIX-SH3/PAK peptide complex and shown that it differs from typical Src-like SH3/peptide complexes. The peptide makes contacts through the Pro-rich sequence in a similar way to standard SH3/peptide complexes, even though the Pro residue positions are not conserved. In addition, there are interactions with a Pro and Lys in the PAK, which are C-terminal to the conserved Arg found in all SH3-binding sequences. These contact a fourth binding pocket on the SH3 domain. We have measured the affinity of PIX-SH3 for the PAK peptide and found that it is of intermediate affinity. When PAK is activated, Ser-199 in the PIX-binding site is phosphorylated. This phosphorylation is sufficient to reduce the affinity for PIX 6-fold.
About this Structure
1ZSG is a Protein complex structure of sequences from Homo sapiens. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)., Mott HR, Nietlispach D, Evetts KA, Owen D, Biochemistry. 2005 Aug 23;44(33):10977-83. PMID:16101281
Page seeded by OCA on Thu Feb 21 16:18:43 2008
