View source for 4kgs


==Backbone Modifications in the Protein GB1 Loops: beta-3-Val21, beta-3-Asp40==
<StructureSection load='4kgs' size='340' side='right'caption='[[4kgs]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kgs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGS 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1VR:(3R)-3-AMINO-4-METHYLPENTANOIC+ACID'>1VR</scene>, <scene name='pdbligand=B3D:3-AMINOPENTANEDIOIC+ACID'>B3D</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=4kgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgs OCA], [https://pdbe.org/4kgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgs RCSB], [https://www.ebi.ac.uk/pdbsum/4kgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Because proteins play vital roles in life, much effort has been invested in their mimicry by synthetic agents. One approach is to design unnatural backbone oligomers ("foldamers") that fold like natural peptides. Despite success in secondary structure mimicry by such species, protein-like tertiary folds remain elusive. A fundamental challenge underlying this task is the design of a sequence of side chains that will specify a complex tertiary folding pattern on an unnatural backbone. We report here a sequence-based approach to convert a natural protein with a compact tertiary fold to an analogue with a backbone composed of approximately 20% unnatural building blocks but folding behavior similar to that of the parent protein.

Protein-like Tertiary Folding Behavior from Heterogeneous Backbones.,Reinert ZE, Lengyel GA, Horne WS J Am Chem Soc. 2013 Aug 28;135(34):12528-31. doi: 10.1021/ja405422v. Epub 2013, Aug 15. PMID:23937097<ref>PMID:23937097</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kgs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus sp. 'group G']]
[[Category: Horne WS]]
[[Category: Lengyel GA]]
[[Category: Reinert ZE]]