8vgl: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 8vgl is ON HOLD
+==CryoEM structure of Nav1.7 in complex with wild type Fab 7A9==
+<StructureSection load='8vgl' size='340' side='right'caption='[[8vgl]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8vgl]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliarcobacter_butzleri_RM4018 Aliarcobacter butzleri RM4018] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VGL FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#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=8vgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vgl OCA], [https://pdbe.org/8vgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vgl RCSB], [https://www.ebi.ac.uk/pdbsum/8vgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vgl ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+High-resolution structures of proteins are critical to understanding molecular mechanisms of biological processes and in the discovery of therapeutic molecules. Cryo-EM has revolutionized structure determination of large proteins and their complexes(1), but a vast majority of proteins that underlie human diseases are small (&lt; 50 kDa) and usually beyond its reach due to low signal-to-noise images and difficulties in particle alignment(2). Current strategies to overcome this problem increase the overall size of small protein targets using scaffold proteins that bind to the target, but are limited by inherent flexibility and not being bound to their targets in a rigid manner, resulting in the target being poorly resolved compared to the scaffolds(3-11). Here we present an iteratively engineered molecular design for transforming Fabs (antibody fragments), into conformationally rigid scaffolds (Rigid-Fabs) that, when bound to small proteins (~20 kDa), can enable high-resolution structure determination using cryo-EM. This design introduces multiple disulfide bonds at strategic locations, generates a well-folded Fab constrained into a rigid conformation and can be applied to Fabs from various species, isotypes and chimeric Fabs. We present examples of the Rigid Fab design enabling high-resolution (2.3-2.5 A) structures of small proteins, Ang2 (26 kDa) and KRAS (21 kDa) by cryo-EM. The strategies for designing disulfide constrained Rigid Fabs in our work thus establish a general approach to overcome the target size limitation of single particle cryo-EM.
-Authors:
+Disulfi de constrained Fabs overcome target size limitation for high-resolution single-particle cryo-EM.,Kung JE, Johnson MC, Jao CC, Arthur CP, Tegunov D, Rohou A, Sudhamsu J bioRxiv [Preprint]. 2024 May 13:2024.05.10.593593. doi: , 10.1101/2024.05.10.593593. PMID:38798381<ref>PMID:38798381</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8vgl" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aliarcobacter butzleri RM4018]]
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Arthur CP]]
+[[Category: Jao CC]]
+[[Category: Kung JE]]
+[[Category: Sudhamsu J]]