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[[Image:1le3.jpg|left|200px]]<br /><applet load="1le3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1le3" />
'''NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G'''<br />


==Overview==
==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.
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.


==About this Structure==
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>
1LE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1HS0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE3 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11331745 11331745]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1le3" style="background-color:#fffaf0;"></div>
[[Category: Cochran, A G.]]
== References ==
[[Category: Skelton, N J.]]
<references/>
[[Category: Starovasnik, M A.]]
__TOC__
[[Category: NH2]]
</StructureSection>
[[Category: beta-hairpin]]
[[Category: Large Structures]]
[[Category: type i beta-turn]]
[[Category: Streptococcus sp. 'group G']]
 
[[Category: Cochran AG]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:08 2008''
[[Category: Skelton NJ]]
[[Category: Starovasnik MA]]

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