5n8b: Difference between revisions
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<StructureSection load='5n8b' size='340' side='right'caption='[[5n8b]], [[Resolution|resolution]] 1.03Å' scene=''> | <StructureSection load='5n8b' size='340' side='right'caption='[[5n8b]], [[Resolution|resolution]] 1.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n8b]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N8B OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5n8b]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N8B FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.03Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=5n8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n8b OCA], [https://pdbe.org/5n8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n8b RCSB], [https://www.ebi.ac.uk/pdbsum/5n8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n8b ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces avidinii]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Albert T]] | ||
[[Category: | [[Category: Bannen R]] | ||
[[Category: | [[Category: Benz J]] | ||
[[Category: Goodrich L]] | |||
[[Category: | [[Category: Lyamichev V]] | ||
[[Category: | [[Category: Patel J]] | ||
[[Category: | [[Category: Sullivan E]] | ||
[[Category: | |||
Latest revision as of 15:34, 15 November 2023
CRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE AFPDYLAEYHGGCRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE AFPDYLAEYHGG
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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