4kgr: Difference between revisions
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== | ==Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35== | ||
[[4kgr]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KGR OCA]. | <StructureSection load='4kgr' size='340' side='right'caption='[[4kgr]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4kgr]] is a 8 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=4KGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KGR 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3A:(3S)-3-AMINOBUTANOIC+ACID'>B3A</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=B3X:(3S)-3,5-DIAMINO-5-OXOPENTANOIC+ACID'>B3X</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=4kgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kgr OCA], [https://pdbe.org/4kgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kgr RCSB], [https://www.ebi.ac.uk/pdbsum/4kgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kgr 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> | |||
<ref | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4kgr" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus sp. 'group G']] | |||
[[Category: Horne WS]] | |||
[[Category: Lengyel GA]] | |||
[[Category: Reinert ZE]] | |||
Latest revision as of 18:59, 20 September 2023
Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35
Structural highlights
FunctionSPG1_STRSG Binds to the constant Fc region of IgG with high affinity. Publication Abstract from PubMedBecause 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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