We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1kff

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kff.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kff.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kff| PDB=1kff | SCENE= }}
{{STRUCTURE_1kff| PDB=1kff | SCENE= }}
-
'''An engineered streptavidin with improved affinity for the strep-tag II peptide: apo-SAM1'''
+
===An engineered streptavidin with improved affinity for the strep-tag II peptide: apo-SAM1===
-
==Overview==
+
<!--
-
The Strep-tag II is a nine-amino acid peptide that was developed as an affinity tool for the purification of corresponding fusion proteins on streptavidin columns. The peptide recognizes the same pocket of streptavidin where the natural ligand is normally bound so that biotin or its chemical derivatives can be used for competitive elution. We report here the crystal structures of the streptavidin mutants '1' and '2,' which had been engineered for 10-fold higher affinity towards the Strep-tag II. Both streptavidin mutants carry mutations at positions 44, 45, and 47, that is, in a flexible loop region close to the binding site. The crystal structures of the two apo-proteins and their complexes with the Strep-tag II peptide were refined at resolutions below 2 A. Both in the presence and absence of the peptide, the lid-like loop next to the ligand pocket--comprising residues 45 through 52--adopts an 'open' conformation in all four subunits within the asymmetric unit. The same loop was previously described to be disordered in the wild-type apo-streptavidin and to close over the pocket upon complexation of the natural ligand biotin. Our findings suggest that stabilization of the 'open' loop conformation in the absence of a ligand abolishes the need for conformational rearrangement prior to the docking of the voluminous peptide. Because no direct contacts between the flexible part of the loop and the peptide ligand were detected, it seems likely that the higher affinity of the two streptavidin mutants for the Strep-tag II is caused by a predominantly entropic mechanism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11910031}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11910031 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11910031}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Strep-tag]]
[[Category: Strep-tag]]
[[Category: Streptavidin]]
[[Category: Streptavidin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:40:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:15:49 2008''

Revision as of 07:15, 2 July 2008

Image:1kff.png

Template:STRUCTURE 1kff

An engineered streptavidin with improved affinity for the strep-tag II peptide: apo-SAM1

Template:ABSTRACT PUBMED 11910031

About this Structure

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

Reference

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site., Korndorfer IP, Skerra A, Protein Sci. 2002 Apr;11(4):883-93. PMID:11910031

Page seeded by OCA on Wed Jul 2 10:15:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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