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2pna
From Proteopedia
(New page: 200px<br /><applet load="2pna" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pna" /> '''STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA ...) |
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'''STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE'''<br /> | '''STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Receptor protein-tyrosine kinases, through phosphorylation of specific | + | Receptor protein-tyrosine kinases, through phosphorylation of specific tyrosine residues, generate high-affinity binding sites which direct assembly of multienzyme signalling complexes. Many of these signalling proteins, including phospholipase C gamma, GTPase-activating protein and phosphatidylinositol-3-OH kinase, contain src-homology 2 (SH2) domains, which bind with high affinity and specificity to tyrosine-phosphorylated sequences. The critical role played by SH2 domains in signalling has been highlighted by recent studies showing that mutation of specific phosphorylation sites on the platelet-derived growth factor receptor impair its association with phosphatidylinositol-3-OH kinase, preventing growth factor-induced mitogenesis. Here we report the solution structure of an isolated SH2 domain from the 85K regulatory subunit of phosphatidylinositol-3-OH kinase, determined using multidimensional nuclear magnetic resonance spectroscopy. The structure is characterized by a central region of beta-sheet flanked by two alpha-helices, with a highly flexible loop close to functionally important residues previously identified by site-directed mutagenesis. |
==About this Structure== | ==About this Structure== | ||
| - | 2PNA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/Phosphatidylinositol_3-kinase Phosphatidylinositol 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.137 2.7.1.137] Full crystallographic information is available from [http:// | + | 2PNA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/Phosphatidylinositol_3-kinase Phosphatidylinositol 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.137 2.7.1.137] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNA OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Phosphatidylinositol 3-kinase]] | [[Category: Phosphatidylinositol 3-kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Booker, G | + | [[Category: Booker, G W.]] |
| - | [[Category: Breeze, A | + | [[Category: Breeze, A L.]] |
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Downing, A | + | [[Category: Downing, A K.]] |
[[Category: Gout, I.]] | [[Category: Gout, I.]] | ||
[[Category: Panayotou, G.]] | [[Category: Panayotou, G.]] | ||
| - | [[Category: Waterfield, M | + | [[Category: Waterfield, M D.]] |
[[Category: signalling protein]] | [[Category: signalling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:13 2008'' |
Revision as of 16:31, 21 February 2008
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STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE
Overview
Receptor protein-tyrosine kinases, through phosphorylation of specific tyrosine residues, generate high-affinity binding sites which direct assembly of multienzyme signalling complexes. Many of these signalling proteins, including phospholipase C gamma, GTPase-activating protein and phosphatidylinositol-3-OH kinase, contain src-homology 2 (SH2) domains, which bind with high affinity and specificity to tyrosine-phosphorylated sequences. The critical role played by SH2 domains in signalling has been highlighted by recent studies showing that mutation of specific phosphorylation sites on the platelet-derived growth factor receptor impair its association with phosphatidylinositol-3-OH kinase, preventing growth factor-induced mitogenesis. Here we report the solution structure of an isolated SH2 domain from the 85K regulatory subunit of phosphatidylinositol-3-OH kinase, determined using multidimensional nuclear magnetic resonance spectroscopy. The structure is characterized by a central region of beta-sheet flanked by two alpha-helices, with a highly flexible loop close to functionally important residues previously identified by site-directed mutagenesis.
About this Structure
2PNA is a Single protein structure of sequence from Bos taurus. Active as Phosphatidylinositol 3-kinase, with EC number 2.7.1.137 Full crystallographic information is available from OCA.
Reference
Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase., Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, Waterfield MD, Campbell ID, Nature. 1992 Aug 20;358(6388):684-7. PMID:1323062
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