3zy7: Difference between revisions
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< | ==Crystal structure of computationally redesigned gamma-adaptin appendage domain forming a symmetric homodimer== | ||
<StructureSection load='3zy7' size='340' side='right'caption='[[3zy7]], [[Resolution|resolution]] 1.09Å' scene=''> | |||
== Structural highlights == | |||
or the | <table><tr><td colspan='2'>[[3zy7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZY7 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.09Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=3zy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zy7 OCA], [https://pdbe.org/3zy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zy7 RCSB], [https://www.ebi.ac.uk/pdbsum/3zy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zy7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AP1G1_MOUSE AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Computational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a beta-strand is thought of as "sticky" and beta-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed beta-strands to form an intermolecular beta-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 A). This work demonstrates that beta-strand pairing can be used to computationally design new interactions with high accuracy. | |||
Computational design of a symmetric homodimer using beta-strand assembly.,Stranges PB, Machius M, Miley MJ, Tripathy A, Kuhlman B Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20562-7. Epub 2011 Dec 5. PMID:22143762<ref>PMID:22143762</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zy7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adaptin 3D structures|Adaptin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | |||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Kuhlman | [[Category: Kuhlman B]] | ||
[[Category: Machius | [[Category: Machius M]] | ||
[[Category: Miley | [[Category: Miley MJ]] | ||
[[Category: Stranges | [[Category: Stranges PB]] | ||
[[Category: Tripathy | [[Category: Tripathy A]] | ||
Latest revision as of 14:15, 20 December 2023
Crystal structure of computationally redesigned gamma-adaptin appendage domain forming a symmetric homodimerCrystal structure of computationally redesigned gamma-adaptin appendage domain forming a symmetric homodimer
Structural highlights
FunctionAP1G1_MOUSE Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Publication Abstract from PubMedComputational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a beta-strand is thought of as "sticky" and beta-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed beta-strands to form an intermolecular beta-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 A). This work demonstrates that beta-strand pairing can be used to computationally design new interactions with high accuracy. Computational design of a symmetric homodimer using beta-strand assembly.,Stranges PB, Machius M, Miley MJ, Tripathy A, Kuhlman B Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20562-7. Epub 2011 Dec 5. PMID:22143762[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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