1uti
From Proteopedia
(New page: 200px<br /><applet load="1uti" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uti, resolution 1.50Å" /> '''MONA/GADS SH3C IN CO...) |
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| - | [[Image:1uti.gif|left|200px]]<br /><applet load="1uti" size=" | + | [[Image:1uti.gif|left|200px]]<br /><applet load="1uti" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uti, resolution 1.50Å" /> | caption="1uti, resolution 1.50Å" /> | ||
'''MONA/GADS SH3C IN COMPLEX WITH HPK DERIVED PEPTIDE'''<br /> | '''MONA/GADS SH3C IN COMPLEX WITH HPK DERIVED PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling | + | Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several prolinerich motifs, which have been shown to interact with different SH3 domain-containing adaptor proteins in vitro. One of these, Mona/Gads, was also shown to bind HPK1 in mouse T cells in vivo. The region of HPK1 that binds to the Mona/Gads C-terminal SH3 domain has been mapped and shows only very limited similarity to a recently identified high affinity binding motif in SLP-76, another T-cell adaptor. Using isothermal titration calorimetry and x-ray crystallography, the binding of the HPK1 motif to Mona/Gads SH3C has now been characterized in molecular detail. The results indicate that although charge interactions through an RXXK motif are essential for complex formation, a PXXP motif in HPK1 strongly complements binding. This unexpected binding mode therefore differs considerably from the previously described interaction of Mona/Gads SH3C with SLP-76. The crystal structure of the complex highlights the great versatility of SH3 domains, which allows interactions with very different proteins. This currently limits our ability to categorize SH3 binding properties by simple rules. |
==About this Structure== | ==About this Structure== | ||
| - | 1UTI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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:// | + | 1UTI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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=1UTI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Domart, M | + | [[Category: Domart, M C.]] |
| - | [[Category: Feller, S | + | [[Category: Feller, S M.]] |
[[Category: Harkiolaki, M.]] | [[Category: Harkiolaki, M.]] | ||
[[Category: Lewitzky, M.]] | [[Category: Lewitzky, M.]] | ||
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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 15:28:07 2008'' |
Revision as of 13:28, 21 February 2008
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MONA/GADS SH3C IN COMPLEX WITH HPK DERIVED PEPTIDE
Overview
Hematopoietic progenitor kinase 1 (HPK1) is implicated in signaling downstream of the T cell receptor. Its non-catalytic, C-terminal half contains several prolinerich motifs, which have been shown to interact with different SH3 domain-containing adaptor proteins in vitro. One of these, Mona/Gads, was also shown to bind HPK1 in mouse T cells in vivo. The region of HPK1 that binds to the Mona/Gads C-terminal SH3 domain has been mapped and shows only very limited similarity to a recently identified high affinity binding motif in SLP-76, another T-cell adaptor. Using isothermal titration calorimetry and x-ray crystallography, the binding of the HPK1 motif to Mona/Gads SH3C has now been characterized in molecular detail. The results indicate that although charge interactions through an RXXK motif are essential for complex formation, a PXXP motif in HPK1 strongly complements binding. This unexpected binding mode therefore differs considerably from the previously described interaction of Mona/Gads SH3C with SLP-76. The crystal structure of the complex highlights the great versatility of SH3 domains, which allows interactions with very different proteins. This currently limits our ability to categorize SH3 binding properties by simple rules.
About this Structure
1UTI is a Protein complex structure of sequences from Mus musculus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix., Lewitzky M, Harkiolaki M, Domart MC, Jones EY, Feller SM, J Biol Chem. 2004 Jul 2;279(27):28724-32. Epub 2004 Apr 20. PMID:15100220
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