8g4e
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g4e OCA], [https://pdbe.org/8g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g4e RCSB], [https://www.ebi.ac.uk/pdbsum/8g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g4e 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=8g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g4e OCA], [https://pdbe.org/8g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g4e RCSB], [https://www.ebi.ac.uk/pdbsum/8g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g4e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cryoelectron microscopy (Cryo-EM) has enabled structural determination of proteins larger than about 50 kDa, including many intractable by any other method, but it has largely failed for smaller proteins. Here, we obtain structures of small proteins by binding them to a rigid molecular scaffold based on a designed protein cage, revealing atomic details at resolutions reaching 2.9 A. We apply this system to the key cancer signaling protein KRAS (19 kDa in size), obtaining four structures of oncogenic mutational variants by cryo-EM. Importantly, a structure for the key G12C mutant bound to an inhibitor drug (AMG510) reveals significant conformational differences compared to prior data in the crystalline state. The findings highlight the promise of cryo-EM scaffolds for advancing the design of drug molecules against small therapeutic protein targets in cancer and other human diseases. | ||
| + | |||
| + | Cryo-EM structure determination of small therapeutic protein targets at 3 A-resolution using a rigid imaging scaffold.,Castells-Graells R, Meador K, Arbing MA, Sawaya MR, Gee M, Cascio D, Gleave E, Debreczeni JE, Breed J, Leopold K, Patel A, Jahagirdar D, Lyons B, Subramaniam S, Phillips C, Yeates TO Proc Natl Acad Sci U S A. 2023 Sep 12;120(37):e2305494120. doi: , 10.1073/pnas.2305494120. Epub 2023 Sep 5. PMID:37669364<ref>PMID:37669364</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8g4e" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Green Fluorescence Protein imaged on a cryo-EM imaging scaffold
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