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5N99

CRYSTAL STRUCTURE OF STREPTAVIDIN with cyclic peptide NQpWQ

Summary for 5N99
Entry DOI10.2210/pdb5n99/pdb
DescriptorStreptavidin, ASN-GLN-DPR-TRP-GLN (3 entities in total)
Functional Keywordsstreptavidin, biotin binding, d-amino acid, streptavidin cyclic peptide complex, biotin binding protein
Biological sourceStreptomyces avidinii
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Cellular locationSecreted: P22629
Total number of polymer chains24
Total formula weight234256.46
Authors
Lyamichev, V.,Goodrich, L.,Sullivan, E.,Bannen, R.,Benz, J.,Albert, T.,Patel, J. (deposition date: 2017-02-24, release date: 2017-10-04)
Primary citationLyamichev, V.I.,Goodrich, L.E.,Sullivan, E.H.,Bannen, R.M.,Benz, J.,Albert, T.J.,Patel, J.J.
Stepwise Evolution Improves Identification of Diverse Peptides Binding to a Protein Target.
Sci Rep, 7:12116-12116, 2017
Cited by
PubMed Abstract: 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.
PubMed: 28935886
DOI: 10.1038/s41598-017-12440-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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