|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5x6h' size='340' side='right'caption='[[5x6h]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5x6h' size='340' side='right'caption='[[5x6h]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x6h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4zl2 4zl2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X6H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x6h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4zl2 4zl2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X6H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x6g|5x6g]], [[5x6m|5x6m]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Smad5, Madh5, Msmad5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5x6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6h OCA], [https://pdbe.org/5x6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x6h RCSB], [https://www.ebi.ac.uk/pdbsum/5x6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6h ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6h OCA], [http://pdbe.org/5x6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x6h RCSB], [http://www.ebi.ac.uk/pdbsum/5x6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SMAD5_MOUSE SMAD5_MOUSE]] Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity). Required for angiogenesis. | + | [https://www.uniprot.org/uniprot/SMAD5_MOUSE SMAD5_MOUSE] Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity). Required for angiogenesis. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chai, N]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Wang, J]] | + | [[Category: Chai N]] |
| - | [[Category: Wang, Z X]] | + | [[Category: Wang J]] |
| - | [[Category: Wu, J W]]
| + | [[Category: Wang ZX]] |
| - | [[Category: Gc-rich dna]] | + | [[Category: Wu JW]] |
| - | [[Category: Metal binding protein-dna complex]] | + | |
| - | [[Category: Smad mh1 domain]]
| + | |
| Structural highlights
Function
SMAD5_MOUSE Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD5 is a receptor-regulated SMAD (R-SMAD) (By similarity). Required for angiogenesis.
Publication Abstract from PubMed
Smad proteins are important intracellular mediators of TGF-beta signalling, which transmit signals directly from cell surface receptors to the nucleus. The MH1 domain of Smad plays a key role in DNA recognition. Two types of DNA sequence were identified as Smad binding motifs: the Smad binding element (SBE) and the GC-rich sequence. Here we report the first crystal structure of the Smad5 MH1 domain in complex with the GC-rich sequence. Compared with the Smad5-MH1/SBE complex structure, the Smad5 MH1 domain contacts the GC-rich site with the same beta-hairpin, but the detailed interaction modes are different. Conserved beta-hairpin residues make base specific contacts with the minimal GC-rich site, 5'-GGC-3'. The assembly of Smad5-MH1 on the GC-rich DNA also results in distinct DNA conformational changes. Moreover, the crystal structure of Smad5-MH1 in complex with a composite DNA sequence demonstrates that the MH1 domain is targeted to each binding site (GC-rich or SBE) with modular binding modes, and the length of the DNA spacer affects the MH1 assembly. In conclusion, our work provides the structural basis for the recognition and binding specificity of the Smad MH1 domain with the DNA targets.
Structural basis for the Smad5 MH1 domain to recognize different DNA sequences.,Chai N, Li WX, Wang J, Wang ZX, Yang SM, Wu JW Nucleic Acids Res. 2015 Aug 24. pii: gkv848. PMID:26304548[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chai N, Li WX, Wang J, Wang ZX, Yang SM, Wu JW. Structural basis for the Smad5 MH1 domain to recognize different DNA sequences. Nucleic Acids Res. 2015 Aug 24. pii: gkv848. PMID:26304548 doi:http://dx.doi.org/10.1093/nar/gkv848
|
