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3gmj

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Revision as of 06:01, 7 December 2018

Crystal structure of MAD MH2 domain

Structural highlights

3gmj is a 4 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Mad (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MAD_DROME] Required for the function of decapentaplegic. May play an important role in mediating Dpp signaling. Involved in the BMP signaling pathway.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The decapentaplegic(Dpp), a member of the TGF-beta superfamily, plays a pivotal role in the control of proliferation, global patterning and induction of specific cell fates during Drosophila development. Mother against Dpp(Mad) is the founding member of the conserved Smad protein family which specifically transduces the intracellular TGF-beta signaling cascade. Here we report the 2.80 A structure of the MH2 domain of Mad(Mad-MH2) that was readily superposed to the mammal Smad-MH2 structures. This unphosphorylated Mad-MH2 forms a symmetric homotrimer in crystals, consistent with the result of the size-exclusion chromatography that Mad-MH2 exhibited a propensity for concentration-dependent oligomerization prior to phosphorylation. Structural analysis revealed that the formation of homotrimeric Mad-MH2 is mainly mediated by contacts involving the extreme C-terminal SSVS motif, and is strengthened by phosphorylation of the last two Ser residues which was confirmed by the gel filtration analysis of the pseudophosphorylated Mad-MH2(DVD). Intriguingly, the homotrimer within an asymmetric unit only possesses two ordered C-terminal tails, reminiscent of the arrangement of the R-Smad/Smad4 complexes, indicating that the subunit with a flexible SSXS motif would be readily replaced by Co-Smad to form a functional heterotrimer.

Crystal structure of the MH2 domain of Drosophila Mad.,WANG C, CHEN L, WANG L, WU J Sci China C Life Sci. 2009 Jun;52(6):539-44. Epub 2009 Jun 26. PMID:19557331^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zeng YA, Rahnama M, Wang S, Sosu-Sedzorme W, Verheyen EM. Drosophila Nemo antagonizes BMP signaling by phosphorylation of Mad and inhibition of its nuclear accumulation. Development. 2007 Jun;134(11):2061-71. PMID:17507407 doi:http://dx.doi.org/134/11/2061
↑ Sekelsky JJ, Newfeld SJ, Raftery LA, Chartoff EH, Gelbart WM. Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster. Genetics. 1995 Mar;139(3):1347-58. PMID:7768443
↑ WANG C, CHEN L, WANG L, WU J. Crystal structure of the MH2 domain of Drosophila Mad. Sci China C Life Sci. 2009 Jun;52(6):539-44. Epub 2009 Jun 26. PMID:19557331 doi:10.1007/s11427-009-0080-x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gmj"

@@ Line 1: / Line 1: @@
 ==Crystal structure of MAD MH2 domain==
 <StructureSection load='3gmj' size='340' side='right' caption='[[3gmj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[3gmj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GMJ FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mad ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmj OCA], [http://pdbe.org/3gmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gmj RCSB], [http://www.ebi.ac.uk/pdbsum/3gmj PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmj OCA], [http://pdbe.org/3gmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gmj RCSB], [http://www.ebi.ac.uk/pdbsum/3gmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gmj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/3gmj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/3gmj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 34: / Line 35: @@
 [[Category: Wang, C]]
 [[Category: Wu, J W]]
+[[Category: Cytoplasm]]
 [[Category: Developmental protein]]
 [[Category: Mad]]
@@ Line 42: / Line 44: @@
 [[Category: Transcription]]
 [[Category: Transcription regulation]]
+[[Category: Ubl conjugation]]

3gmj

From Proteopedia

Revision as of 06:01, 7 December 2018

Crystal structure of MAD MH2 domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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