1dev: Difference between revisions

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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"

<applet load="1dev" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1dev, resolution 2.2Å" />

'''CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA'''<br />

==Overview==

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.

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==

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]], Chylomicron retention disease with Marinesco-Sjogren syndrome~~ 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]]

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==

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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DEV OCA].

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==

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[[Category: three-helix bundle]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:31:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:56 2008''

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@@ Line 1: / Line 1: @@
-[[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"
-<applet load="1dev" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1dev, resolution 2.2&Aring;" />
 '''CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA'''<br />
 ==Overview==
-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.
+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==
-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]], Chylomicron retention disease with Marinesco-Sjogren syndrome 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]]
+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==
-DEV 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEV OCA].
+DEV 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==
@@ Line 22: / Line 21: @@
 [[Category: three-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:31:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:56 2008''