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3dit

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Current revision

Crystal structure of MAD MH2 domain

Structural highlights

3dit is a 3 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
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

In Drosophila, decapentaplegic (Dpp), a member of the TGF-beta superfamily, plays a pivotal role in control of proliferation, global patterning and induction of specific cell fates. Together with Medea, mother against Dpp (Mad), the founding member of the Smad family, specifically transduces the Dpp signal from the plasma membrane to the nucleus. Here, the crystal structure of the MH2 domain of Mad, which closely matches those of other Smad MH2 domains, is reported at 3.2 A resolution. The conservation of Smad protein structures is consistent with their evolutionary conserved and significant function. Furthermore, sequence alignment revealed that most of the variant amino acids in Smad proteins specific to the BMP pathway (Smad1, Smad5 and Mad) were clustered at the surface. In particular, Ser296 and Asp297 of Mad introduced a negative patch into the positive surface observed in the surface electrostatic potential of Smad1 MH2.

Structure of Drosophila Mad MH2 domain.,Hao R, Chen L, Wu JW, Wang ZX Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt, 11):986-90. Epub 2008 Oct 31. PMID:18997322^[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
↑ Hao R, Chen L, Wu JW, Wang ZX. Structure of Drosophila Mad MH2 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt, 11):986-90. Epub 2008 Oct 31. PMID:18997322 doi:10.1107/S1744309108033034

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/3dit"

Categories: Drosophila melanogaster | Large Structures | Hao R | Wang ZX | Wu JW

@@ Line 3: / Line 3: @@
 <StructureSection load='3dit' size='340' side='right'caption='[[3dit]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3dit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3dit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DIT FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mad, CG12399 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dit OCA], [https://pdbe.org/3dit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dit RCSB], [https://www.ebi.ac.uk/pdbsum/3dit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dit ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MAD_DROME MAD_DROME]] Required for the function of decapentaplegic. May play an important role in mediating Dpp signaling. Involved in the BMP signaling pathway.<ref>PMID:17507407</ref> <ref>PMID:7768443</ref>
+[https://www.uniprot.org/uniprot/MAD_DROME MAD_DROME] Required for the function of decapentaplegic. May play an important role in mediating Dpp signaling. Involved in the BMP signaling pathway.<ref>PMID:17507407</ref> <ref>PMID:7768443</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Hao, R]]
+[[Category: Hao R]]
-[[Category: Wang, Z X]]
+[[Category: Wang ZX]]
-[[Category: Wu, J W]]
+[[Category: Wu JW]]
-[[Category: Cytoplasm]]
-[[Category: Developmental protein]]
-[[Category: Mad]]
-[[Category: Mh2]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Signaling protein]]
-[[Category: Tgf-beta]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Ubl conjugation]]

3dit

From Proteopedia

Current revision

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?)

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