1q2h
From Proteopedia
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| - | [[Image:1q2h.gif|left|200px]] | + | [[Image:1q2h.gif|left|200px]] |
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| - | '''Phenylalanine Zipper Mediates APS Dimerization''' | + | {{Structure |
| + | |PDB= 1q2h |SIZE=350|CAPTION= <scene name='initialview01'>1q2h</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= APS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Phenylalanine Zipper Mediates APS Dimerization''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q2H is a [ | + | 1Q2H is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15378031 15378031] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''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 13:32:06 2008'' |
Revision as of 11:32, 20 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | APS (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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