1le3: Difference between revisions
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==NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G== | |||
<StructureSection load='1le3' size='340' side='right'caption='[[1le3]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1le3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hs0 1hs0]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LE3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le3 OCA], [https://pdbe.org/1le3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1le3 RCSB], [https://www.ebi.ac.uk/pdbsum/1le3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1le3 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 == | |||
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks. | |||
Tryptophan zippers: stable, monomeric beta -hairpins.,Cochran AG, Skelton NJ, Starovasnik MA Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745<ref>PMID:11331745</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1le3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: | [[Category: Streptococcus sp. 'group G']] | ||
[[Category: | [[Category: Cochran AG]] | ||
[[Category: | [[Category: Skelton NJ]] | ||
[[Category: | [[Category: Starovasnik MA]] | ||
[[Category: | |||
Latest revision as of 13:28, 16 August 2023
NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein GNMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G
Structural highlights
FunctionSPG1_STRSG Binds to the constant Fc region of IgG with high affinity. Publication Abstract from PubMedA structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks. Tryptophan zippers: stable, monomeric beta -hairpins.,Cochran AG, Skelton NJ, Starovasnik MA Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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