2pnb

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(New page: 200px<br /><applet load="2pnb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pnb" /> '''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==
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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.
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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==
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2PNB 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PNB OCA].
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2PNB 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=2PNB OCA].
==Reference==
==Reference==
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[[Category: Phosphatidylinositol 3-kinase]]
[[Category: Phosphatidylinositol 3-kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Booker, G.W.]]
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[[Category: Booker, G W.]]
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[[Category: Breeze, A.L.]]
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[[Category: Breeze, A L.]]
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[[Category: Campbell, I.D.]]
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[[Category: Campbell, I D.]]
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[[Category: Downing, A.K.]]
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[[Category: Downing, A K.]]
[[Category: Gout, I.]]
[[Category: Gout, I.]]
[[Category: Panayotou, G.]]
[[Category: Panayotou, G.]]
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[[Category: Waterfield, M.D.]]
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[[Category: Waterfield, M D.]]
[[Category: signalling protein]]
[[Category: signalling protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:36:04 2007''
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''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


2pnb

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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

2PNB 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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