4r58

</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=4r58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r58 OCA], [https://pdbe.org/4r58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r58 RCSB], [https://www.ebi.ac.uk/pdbsum/4r58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r58 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Shape complementarity is an important component of molecular recognition, and the ability to precisely adjust the shape of a binding scaffold to match a target of interest would greatly facilitate the creation of high-affinity protein reagents and therapeutics. Here we describe a general approach to control the shape of the binding surface on repeat-protein scaffolds and apply it to leucine-rich-repeat proteins. First, self-compatible building-block modules are designed that, when polymerized, generate surfaces with unique but constant curvatures. Second, a set of junction modules that connect the different building blocks are designed. Finally, new proteins with custom-designed shapes are generated by appropriately combining building-block and junction modules. Crystal structures of the designs illustrate the power of the approach in controlling repeat-protein curvature.

Control of repeat-protein curvature by computational protein design.,Park K, Shen BW, Parmeggiani F, Huang PS, Stoddard BL, Baker D Nat Struct Mol Biol. 2015 Jan 12. doi: 10.1038/nsmb.2938. PMID:25580576<ref>PMID:25580576</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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