1y1u
From Proteopedia
(New page: 200px<br /><applet load="1y1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y1u, resolution 3.21Å" /> '''Structure of unphosp...) |
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| - | [[Image:1y1u.gif|left|200px]]<br /><applet load="1y1u" size=" | + | [[Image:1y1u.gif|left|200px]]<br /><applet load="1y1u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y1u, resolution 3.21Å" /> | caption="1y1u, resolution 3.21Å" /> | ||
'''Structure of unphosphorylated STAT5a'''<br /> | '''Structure of unphosphorylated STAT5a'''<br /> | ||
==Overview== | ==Overview== | ||
| - | STAT proteins have the function of signaling from the cell membrane into | + | STAT proteins have the function of signaling from the cell membrane into the nucleus, where they regulate gene transcription. Latent mammalian STAT proteins can form dimers in the cytoplasm even before receptor-mediated activation by specific tyrosine phosphorylation. Here we describe the 3.21-A crystal structure of an unphosphorylated STAT5a homodimer lacking the N-terminal domain as well as the C-terminal transactivation domain. The overall structure of this fragment is very similar to phosphorylated STATs. However, important differences exist in the dimerization mode. Although the interface between phosphorylated STATs is mediated by their Src-homology 2 domains, the unphosphorylated STAT5a fragment dimerizes in a completely different manner via interactions between their beta-barrel and four-helix bundle domains. The STAT4 N-terminal domain dimer can be docked onto this STAT5a core fragment dimer based on shape and charge complementarities. The separation of the dimeric arrangement, taking place upon activation and nuclear translocation of STAT5a, is demonstrated by fluorescence resonance energy transfer experiments in living cells. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1Y1U is a [http://en.wikipedia.org/wiki/Single_protein 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=1Y1U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Becker, S.]] | [[Category: Becker, S.]] | ||
[[Category: Klumpp, K.]] | [[Category: Klumpp, K.]] | ||
| - | [[Category: Neculai, A | + | [[Category: Neculai, A M.]] |
[[Category: Neculai, D.]] | [[Category: Neculai, D.]] | ||
[[Category: Pfitzner, E.]] | [[Category: Pfitzner, E.]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:58 2008'' |
Revision as of 14:01, 21 February 2008
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Structure of unphosphorylated STAT5a
Overview
STAT proteins have the function of signaling from the cell membrane into the nucleus, where they regulate gene transcription. Latent mammalian STAT proteins can form dimers in the cytoplasm even before receptor-mediated activation by specific tyrosine phosphorylation. Here we describe the 3.21-A crystal structure of an unphosphorylated STAT5a homodimer lacking the N-terminal domain as well as the C-terminal transactivation domain. The overall structure of this fragment is very similar to phosphorylated STATs. However, important differences exist in the dimerization mode. Although the interface between phosphorylated STATs is mediated by their Src-homology 2 domains, the unphosphorylated STAT5a fragment dimerizes in a completely different manner via interactions between their beta-barrel and four-helix bundle domains. The STAT4 N-terminal domain dimer can be docked onto this STAT5a core fragment dimer based on shape and charge complementarities. The separation of the dimeric arrangement, taking place upon activation and nuclear translocation of STAT5a, is demonstrated by fluorescence resonance energy transfer experiments in living cells.
About this Structure
1Y1U is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the unphosphorylated STAT5a dimer., Neculai D, Neculai AM, Verrier S, Straub K, Klumpp K, Pfitzner E, Becker S, J Biol Chem. 2005 Dec 9;280(49):40782-7. Epub 2005 Sep 28. PMID:16192273
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