5m72: Difference between revisions

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<StructureSection load='5m72' size='340' side='right'caption='[[5m72]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5m72' size='340' side='right'caption='[[5m72]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5m72]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M72 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M72 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5m72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M72 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRP72 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SRP68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m72 OCA], [http://pdbe.org/5m72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m72 RCSB], [http://www.ebi.ac.uk/pdbsum/5m72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m72 ProSAT]</span></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=5m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m72 OCA], [https://pdbe.org/5m72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m72 RCSB], [https://www.ebi.ac.uk/pdbsum/5m72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m72 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN]] Autosomal dominant aplasia and myelodysplasia. The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN] Autosomal dominant aplasia and myelodysplasia. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. [[http://www.uniprot.org/uniprot/SRP68_HUMAN SRP68_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.  
[https://www.uniprot.org/uniprot/SRP72_HUMAN SRP72_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Signal recognition particle protein|Signal recognition particle protein]]
*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Becker, M M.M]]
[[Category: Becker MMM]]
[[Category: Sinning, I]]
[[Category: Sinning I]]
[[Category: Wild, K]]
[[Category: Wild K]]
[[Category: Protein targeting]]
[[Category: Protein transport]]
[[Category: Protein-peptide complex]]
[[Category: Signal recognition particle]]
[[Category: Tetratricopeptide repeat]]