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| | ==Crystal structure of the human Mortalin (GRP75) ATPase domain in the apo form== | | ==Crystal structure of the human Mortalin (GRP75) ATPase domain in the apo form== |
| - | <StructureSection load='4kbo' size='340' side='right' caption='[[4kbo]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4kbo' size='340' side='right'caption='[[4kbo]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kbo]] is a 1 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=4KBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KBO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kbo]] is a 1 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=4KBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KBO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2e88|2e88]], [[3atu|3atu]]</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=4kbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kbo OCA], [https://pdbe.org/4kbo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kbo RCSB], [https://www.ebi.ac.uk/pdbsum/4kbo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kbo ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP75, HSPA9, HSPA9B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4kbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kbo OCA], [http://pdbe.org/4kbo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kbo RCSB], [http://www.ebi.ac.uk/pdbsum/4kbo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kbo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GRP75_HUMAN GRP75_HUMAN]] Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. | + | [https://www.uniprot.org/uniprot/GRP75_HUMAN GRP75_HUMAN] Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Amick, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Misra, S]] | + | [[Category: Amick J]] |
| - | [[Category: Nix, J C]]
| + | [[Category: Misra S]] |
| - | [[Category: Page, R C]] | + | [[Category: Nix JC]] |
| - | [[Category: Atp binding]] | + | [[Category: Page RC]] |
| - | [[Category: Atpase]] | + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
GRP75_HUMAN Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone.
Publication Abstract from PubMed
Mortalin, a member of the Hsp70-family of molecular chaperones, functions in a variety of processes including mitochondrial protein import and quality control, Fe-S cluster protein biogenesis, mitochondrial homeostasis, and regulation of p53. Mortalin is implicated in regulation of apoptosis, cell stress response, neurodegeneration, and cancer and is a target of the antitumor compound MKT-077. Like other Hsp70-family members, Mortalin consists of a nucleotide-binding domain (NBD) and a substrate-binding domain. We determined the crystal structure of the NBD of human Mortalin at 2.8 A resolution. Although the Mortalin nucleotide-binding pocket is highly conserved relative to other Hsp70 family members, we find that its nucleotide affinity is weaker than that of Hsc70. A Parkinson's disease-associated mutation is located on the Mortalin-NBD surface and may contribute to Mortalin aggregation. We present structure-based models for how the Mortalin-NBD may interact with the nucleotide exchange factor GrpEL1, with p53, and with MKT-077. Our structure may contribute to the understanding of disease-associated Mortalin mutations and to improved Mortalin-targeting antitumor compounds.
Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone.,Amick J, Schlanger SE, Wachnowsky C, Moseng MA, Emerson CC, Dare M, Luo WI, Ithychanda SS, Nix JC, Cowan JA, Page RC, Misra S Protein Sci. 2014 Mar 29. doi: 10.1002/pro.2466. PMID:24687350[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Amick J, Schlanger SE, Wachnowsky C, Moseng MA, Emerson CC, Dare M, Luo WI, Ithychanda SS, Nix JC, Cowan JA, Page RC, Misra S. Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone. Protein Sci. 2014 Mar 29. doi: 10.1002/pro.2466. PMID:24687350 doi:http://dx.doi.org/10.1002/pro.2466
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