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2g35
From Proteopedia
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| - | [[Image:2g35.gif|left|200px]] | + | [[Image:2g35.gif|left|200px]] |
| - | + | ||
| - | '''NMR structure of talin-PTB in complex with PIPKI''' | + | {{Structure |
| + | |PDB= 2g35 |SIZE=350|CAPTION= <scene name='initialview01'>2g35</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Tln1, Tln ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''NMR structure of talin-PTB in complex with PIPKI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G35 is a [ | + | 2G35 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G35 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the phosphorylation-regulated focal adhesion targeting of type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma) by talin., Kong X, Wang X, Misra S, Qin J, J Mol Biol. 2006 May 26;359(1):47-54. Epub 2006 Mar 23. PMID:[http:// | + | Structural basis for the phosphorylation-regulated focal adhesion targeting of type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma) by talin., Kong X, Wang X, Misra S, Qin J, J Mol Biol. 2006 May 26;359(1):47-54. Epub 2006 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16616931 16616931] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: talin]] | [[Category: talin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:59:49 2008'' |
Revision as of 14:59, 20 March 2008
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| Gene: | Tln1, Tln (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of talin-PTB in complex with PIPKI
Overview
Phosphatidylinositol-4,5-bisphosphate (PIP2) is a key lipid messenger that regulates myriad diverse cellular signaling pathways. To ensure specificity in disparate cellular events, PIP2 must be localized to specific sub-cellular sites. At PIP2-regulated focal adhesion (FA) sites, such localization is in part mediated via the recruitment and activation of PIP2-producing enzyme, type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma), by a phosphotyrosine binding (PTB) domain of talin. Transient phosphorylation of PIPKIgamma at Y644 regulates the interaction and efficient FA targeting of PIPKIgamma; however, the underlying structural basis remains elusive. We have determined the NMR structure of talin-1 PTB in complex with the Y644-phosphorylated PIPKIgamma fragment (WVpYSPLH). As compared to canonical PTB domains that typically recognize the NPXpY turn motif from a variety of signaling proteins, our structure displays an unusual non-NPXpY-based recognition mode for talin-1 PTB where K(357)RW in beta5 strand forms an antiparallel beta-sheet with the VpYS of PIPKIgamma. A specific electrostatic triad between K357/R358 of talin-1 PTB and the pY644 of PIPKIgamma was observed, which is consistent with the mutagenesis and isothermal calorimetry data. Combined with previous in vivo data, our results provide a framework for understanding how phosphorylation of Y644 in PIPKIgamma promotes its specific interaction with talin-1, leading to efficient local synthesis of PIP2 and dynamic regulation of integrin-mediated FA assembly.
About this Structure
2G35 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for the phosphorylation-regulated focal adhesion targeting of type Igamma phosphatidylinositol phosphate kinase (PIPKIgamma) by talin., Kong X, Wang X, Misra S, Qin J, J Mol Biol. 2006 May 26;359(1):47-54. Epub 2006 Mar 23. PMID:16616931
Page seeded by OCA on Thu Mar 20 16:59:49 2008
Categories: Mus musculus | Single protein | Kong, X. | Misra, S. | Qin, J. | Wang, X. | Pipki | Ptb domain | Talin
