1dev: Difference between revisions
New page: left|200px<br /> <applet load="1dev" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dev, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1dev.gif|left|200px]]<br /> | [[Image:1dev.gif|left|200px]]<br /><applet load="1dev" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA'''<br /> | '''CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA'''<br /> | ||
==Overview== | ==Overview== | ||
The Smad proteins mediate transforming growth factor-beta (TGFbeta) | The Smad proteins mediate transforming growth factor-beta (TGFbeta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to the TGFbeta receptors for phosphorylation. The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution. SARA SBD, in an extended conformation comprising a rigid coil, an alpha helix, and a beta strand, interacts with the beta sheet and the three-helix bundle of Smad2. Recognition between the SARA rigid coil and the Smad2 beta sheet is essential for specificity, whereas interactions between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding affinity. Comparison of the structures between Smad2 and a comediator Smad suggests a model for how receptor-regulated Smads are recognized by the type I receptors. | ||
==Disease== | ==Disease== | ||
Known diseases associated with this structure: Anderson disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607690 607690]], Chylomicron retention disease | Known diseases associated with this structure: Anderson disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607690 607690]], Chylomicron retention disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607690 607690]], Mowat-Wilson syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605802 605802]] | ||
==About this Structure== | ==About this Structure== | ||
1DEV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1DEV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DEV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:56 2008'' | ||
Revision as of 13:15, 21 February 2008
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CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA
OverviewOverview
The Smad proteins mediate transforming growth factor-beta (TGFbeta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to the TGFbeta receptors for phosphorylation. The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution. SARA SBD, in an extended conformation comprising a rigid coil, an alpha helix, and a beta strand, interacts with the beta sheet and the three-helix bundle of Smad2. Recognition between the SARA rigid coil and the Smad2 beta sheet is essential for specificity, whereas interactions between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding affinity. Comparison of the structures between Smad2 and a comediator Smad suggests a model for how receptor-regulated Smads are recognized by the type I receptors.
DiseaseDisease
Known diseases associated with this structure: Anderson disease OMIM:[607690], Chylomicron retention disease OMIM:[607690], Mowat-Wilson syndrome OMIM:[605802]
About this StructureAbout this Structure
1DEV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of Smad2 recognition by the Smad anchor for receptor activation., Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massague J, Shi Y, Science. 2000 Jan 7;287(5450):92-7. PMID:10615055
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