5n89: Difference between revisions
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<table><tr><td colspan='2'>[[5n89]] is a 16 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=5N89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N89 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5n89]] is a 16 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=5N89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N89 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]] 1.27Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27Å</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=5n89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n89 OCA], [https://pdbe.org/5n89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n89 RCSB], [https://www.ebi.ac.uk/pdbsum/5n89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n89 ProSAT]</span></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=5n89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n89 OCA], [https://pdbe.org/5n89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n89 RCSB], [https://www.ebi.ac.uk/pdbsum/5n89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n89 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 09:15, 11 September 2024
CRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE GNSFDDWLASKGCRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE GNSFDDWLASKG
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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