5n7x: Difference between revisions
New page: '''Unreleased structure''' The entry 5n7x is ON HOLD Authors: Lyamichev, V., Goodrich, L., Sullivan, E., Bannen, R., Benz, J., Albert, T., Patel, J. Description: CRYSTAL STRUCTURE OF S... |
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The | ==CRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE EWVHPQFEQKAK== | ||
<StructureSection load='5n7x' size='340' side='right'caption='[[5n7x]], [[Resolution|resolution]] 1.12Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n7x]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N7X 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]] 1.12Å</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=5n7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n7x OCA], [https://pdbe.org/5n7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n7x RCSB], [https://www.ebi.ac.uk/pdbsum/5n7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n7x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Considerable efforts have been made to develop technologies for selection of peptidic molecules that act as substrates or binders to a protein of interest. Here we demonstrate the combination of rational peptide array library design, parallel screening and stepwise evolution, to discover novel peptide hotspots. These hotspots can be systematically evolved to create high-affinity, high-specificity binding peptides to a protein target in a reproducible and digitally controlled process. The method can be applied to synthesize both linear and cyclic peptides, as well as peptides composed of natural and non-natural amino acid analogs, thereby enabling screens in a much diverse chemical space. We apply this method to stepwise evolve peptide binders to streptavidin, a protein studied for over two decades and report novel peptides that mimic key interactions of biotin to streptavidin. | |||
Stepwise Evolution Improves Identification of Diverse Peptides Binding to a Protein Target.,Lyamichev VI, Goodrich LE, Sullivan EH, Bannen RM, Benz J, Albert TJ, Patel JJ Sci Rep. 2017 Sep 21;7(1):12116. doi: 10.1038/s41598-017-12440-1. PMID:28935886<ref>PMID:28935886</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5n7x" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Benz | *[[Avidin 3D structures|Avidin 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Patel | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces avidinii]] | |||
[[Category: Albert T]] | |||
[[Category: Bannen R]] | |||
[[Category: Benz J]] | |||
[[Category: Goodrich L]] | |||
[[Category: Lyamichev V]] | |||
[[Category: Patel J]] | |||
[[Category: Sullivan E]] | |||
Latest revision as of 15:32, 15 November 2023
CRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE EWVHPQFEQKAKCRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE EWVHPQFEQKAK
Structural highlights
FunctionSAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedConsiderable efforts have been made to develop technologies for selection of peptidic molecules that act as substrates or binders to a protein of interest. Here we demonstrate the combination of rational peptide array library design, parallel screening and stepwise evolution, to discover novel peptide hotspots. These hotspots can be systematically evolved to create high-affinity, high-specificity binding peptides to a protein target in a reproducible and digitally controlled process. The method can be applied to synthesize both linear and cyclic peptides, as well as peptides composed of natural and non-natural amino acid analogs, thereby enabling screens in a much diverse chemical space. We apply this method to stepwise evolve peptide binders to streptavidin, a protein studied for over two decades and report novel peptides that mimic key interactions of biotin to streptavidin. Stepwise Evolution Improves Identification of Diverse Peptides Binding to a Protein Target.,Lyamichev VI, Goodrich LE, Sullivan EH, Bannen RM, Benz J, Albert TJ, Patel JJ Sci Rep. 2017 Sep 21;7(1):12116. doi: 10.1038/s41598-017-12440-1. PMID:28935886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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