This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sts

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sts.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sts.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sts| PDB=1sts | SCENE= }}
{{STRUCTURE_1sts| PDB=1sts | SCENE= }}
-
'''STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-NH2 DIMER'''
+
===STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-NH2 DIMER===
-
==Overview==
+
<!--
-
Recently, a cyclic peptide ligand, cyclo-Ac-[CHPQG-PPC]-NH2, that binds to streptavidin with high affinity was discovered by screening phage libraries. From the streptavidin-bound crystal structures of cyclo-Ac-[CHPQGPPC]-NH2 and of a related but more weakly binding linear ligand, FSHPQNT, we designed linear thiol-containing streptavidin binding ligands, FCH-PQNT-NH2 and Ac-CHPQNT-NH2, which are dimerized catalytically by the streptavidin crystal lattice of space group I222, as demonstrated by high performance liquid chromatography and mass spectrometry. The catalytic dimerization relies on presentation of the ligand thiols toward one another in the lattice. The streptavidin crystal lattice-mediated catalysis achieved by structure-based design is the first example of catalysis of a chemical reaction by a protein crystal lattice. The spontaneous and crystal catalyzed rates of disulfide formation were determined by high performance liquid chromatography at pH 3.1, 4.0, 5.0, and 6.0. The ratio of the catalyzed to uncatalyzed rate was maximal at pH 3.1 (kcat/kuncat = 3.8), diminishing to 1.2 at pH 6.0. The crystal structures of the streptavidin-bound dimerized peptide ligands, FCHPQNT-NH2 dimer at 1.95 A and Ac-CHPQNT-NH2 dimer at 1.80 A, are described and compared with the structures of streptavidin-bound FSHPQNT monomer and cyclo-Ac-[CHPQGPPC]-NH2 dimer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8537386}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8537386 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8537386}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Katz, B A.]]
[[Category: Katz, B A.]]
[[Category: Liu, B.]]
[[Category: Liu, B.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:07:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:37:13 2008''

Revision as of 12:37, 28 July 2008

Image:1sts.png

Template:STRUCTURE 1sts

STREPTAVIDIN DIMERIZED BY DISULFIDE-BONDED PEPTIDE FCHPQNT-NH2 DIMER

Template:ABSTRACT PUBMED 8537386

About this Structure

1STS is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.

Reference

Topochemical catalysis achieved by structure-based ligand design., Katz BA, Cass RT, Liu B, Arze R, Collins N, J Biol Chem. 1995 Dec 29;270(52):31210-8. PMID:8537386

Page seeded by OCA on Mon Jul 28 15:37:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sts"
Personal tools