1pts
From Proteopedia
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| - | [[Image:1pts.gif|left|200px]] | + | [[Image:1pts.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AND LIGAND BINDING STUDIES OF A SCREENED PEPTIDE COMPLEXED WITH STREPTAVIDIN''' | + | {{Structure |
| + | |PDB= 1pts |SIZE=350|CAPTION= <scene name='initialview01'>1pts</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE AND LIGAND BINDING STUDIES OF A SCREENED PEPTIDE COMPLEXED WITH STREPTAVIDIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PTS is a [ | + | 1PTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTS OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin., Weber PC, Pantoliano MW, Thompson LD, Biochemistry. 1992 Oct 6;31(39):9350-4. PMID:[http:// | + | Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin., Weber PC, Pantoliano MW, Thompson LD, Biochemistry. 1992 Oct 6;31(39):9350-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1390720 1390720] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces avidinii]] | [[Category: Streptomyces avidinii]] | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:56 2008'' |
Revision as of 11:28, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AND LIGAND BINDING STUDIES OF A SCREENED PEPTIDE COMPLEXED WITH STREPTAVIDIN
Overview
The thermodynamic binding parameters and crystal structure for streptavidin-peptide complexes where the peptide sequences were obtained by random screening methods are reported. The affinities between streptavidin and two heptapeptides were determined by titrating calorimetric methods [Phe-Ser-His-Pro-Gln-Asn-Thr, Ka = 7944 (+/- 224) M-1, delta G degrees = -5.32 (+/- 0.01) kcal/mol, and delta H degrees = -19.34 (+/- 0.48) kcal/mol; His-Asp-His-Pro-Gln-Asn-Leu, Ka = 3542 (+/- 146) M-1, delta G degrees = -4.84 (+/- 0.03) kcal/mol, and delta H degrees = -19.00 (+/- 0.64) kcal/mol]. The crystal structure of streptavidin complexed with one of these peptides has been determined at 2.0-A resolution. The peptide (Phe-Ser-His-Pro-Gln-Asn-Thr) binds in a turn conformation with the histidine, proline, and glutamine side chains oriented inward at the biotin-binding site. A water molecule is immobilized between the histidine and glutamine side chains of the peptide and an aspartic acid side chain of the protein. Although some of the residues that participate in binding biotin also interact with the screened peptide, the peptide adopts an alternate method of utilizing binding determinants in the biotin-binding site of streptavidin.
About this Structure
1PTS is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.
Reference
Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin., Weber PC, Pantoliano MW, Thompson LD, Biochemistry. 1992 Oct 6;31(39):9350-4. PMID:1390720
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