1q2h

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(New page: 200px<br /> <applet load="1q2h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2h, resolution 1.70&Aring;" /> '''Phenylalanine Zippe...)
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caption="1q2h, resolution 1.70&Aring;" />
'''Phenylalanine Zipper Mediates APS Dimerization'''<br />
'''Phenylalanine Zipper Mediates APS Dimerization'''<br />
==Overview==
==Overview==
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The APS, SH2-B and LNK proteins are adapters that activate and modulate, receptor tyrosine kinase and JAK/STAT signaling. We now show that a, conserved N-terminal domain mediates APS homodimerization. We determined, the crystal structure of the dimerization domain at a resolution of 1.7 A, using bromide ion MAD phasing. Each molecule contributes two helices to a, compact four-helix bundle having a bisecting-U topology. Its most, conspicuous feature is a stack of interdigitated phenylalanine side chains, at the domain core. These residues create a new motif we refer to as a, 'phenylalanine zipper,' which is critical to dimerization. A newly, developed bridging yeast tri-hybrid assay showed that APS dimerizes JAK2, insulin receptor and IGF1 receptor kinases using its SH2 and dimerization, domains. Dimerization via the phenylalanine zipper domain provides a, mechanism for activating and modulating tyrosine kinase activity even in, the absence of extracellular ligands.
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The APS, SH2-B and LNK proteins are adapters that activate and modulate receptor tyrosine kinase and JAK/STAT signaling. We now show that a conserved N-terminal domain mediates APS homodimerization. We determined the crystal structure of the dimerization domain at a resolution of 1.7 A using bromide ion MAD phasing. Each molecule contributes two helices to a compact four-helix bundle having a bisecting-U topology. Its most conspicuous feature is a stack of interdigitated phenylalanine side chains at the domain core. These residues create a new motif we refer to as a 'phenylalanine zipper,' which is critical to dimerization. A newly developed bridging yeast tri-hybrid assay showed that APS dimerizes JAK2, insulin receptor and IGF1 receptor kinases using its SH2 and dimerization domains. Dimerization via the phenylalanine zipper domain provides a mechanism for activating and modulating tyrosine kinase activity even in the absence of extracellular ligands.
==About this Structure==
==About this Structure==
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1Q2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q2H OCA].
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1Q2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2H OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chi, Y.I.]]
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[[Category: Chi, Y I.]]
[[Category: Dhe-Paganon, S.]]
[[Category: Dhe-Paganon, S.]]
[[Category: Nishi, M.]]
[[Category: Nishi, M.]]
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[[Category: Shoelson, S.E.]]
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[[Category: Shoelson, S E.]]
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[[Category: Werner, E.D.]]
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[[Category: Werner, E D.]]
[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:49:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:16 2008''

Revision as of 12:35, 21 February 2008


1q2h, resolution 1.70Å

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Phenylalanine Zipper Mediates APS Dimerization

Overview

The APS, SH2-B and LNK proteins are adapters that activate and modulate receptor tyrosine kinase and JAK/STAT signaling. We now show that a conserved N-terminal domain mediates APS homodimerization. We determined the crystal structure of the dimerization domain at a resolution of 1.7 A using bromide ion MAD phasing. Each molecule contributes two helices to a compact four-helix bundle having a bisecting-U topology. Its most conspicuous feature is a stack of interdigitated phenylalanine side chains at the domain core. These residues create a new motif we refer to as a 'phenylalanine zipper,' which is critical to dimerization. A newly developed bridging yeast tri-hybrid assay showed that APS dimerizes JAK2, insulin receptor and IGF1 receptor kinases using its SH2 and dimerization domains. Dimerization via the phenylalanine zipper domain provides a mechanism for activating and modulating tyrosine kinase activity even in the absence of extracellular ligands.

About this Structure

1Q2H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A phenylalanine zipper mediates APS dimerization., Dhe-Paganon S, Werner ED, Nishi M, Hansen L, Chi YI, Shoelson SE, Nat Struct Mol Biol. 2004 Oct;11(10):968-74. Epub 2004 Sep 19. PMID:15378031

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