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.


1n0s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1n0s.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1n0s.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n0s| PDB=1n0s | SCENE= }}
{{STRUCTURE_1n0s| PDB=1n0s | SCENE= }}
-
'''ENGINEERED LIPOCALIN FLUA IN COMPLEX WITH FLUORESCEIN'''
+
===ENGINEERED LIPOCALIN FLUA IN COMPLEX WITH FLUORESCEIN===
-
==Overview==
+
<!--
-
The artificial lipocalin FluA with novel specificity toward fluorescein was derived via combinatorial engineering from the bilin-binding protein, BBP by exchange of 16 amino acids in the ligand pocket. Here, we describe the crystal structure of FluA at 2.0 A resolution in the space group P2(1) with two protein-ligand complexes in the asymmetric unit. In both molecules, the characteristic beta-barrel architecture with the attached alpha-helix is well preserved. In contrast, the four loops at one end of the beta-barrel that form the entrance to the binding site exhibit large conformational deviations from the wild-type protein, which can be attributed to the sidechain replacements. Specificity for the new ligand is furnished by hydrophobic packing, charged sidechain environment, and hydrogen bonds with its hydroxyl groups. Unexpectedly, fluorescein is bound in a much deeper cavity than biliverdin IX(gamma) in the natural lipocalin. Triggered by the substituted residues, unmutated sidechains at the bottom of the binding site adopt conformations that are quite different from those observed in the BBP, illustrating that not only the loop region but also the hydrophobic interior of the beta-barrel can be reshaped for molecular recognition. Particularly, Trp 129 participates in a tight stacking interaction with the xanthenolone moiety, which may explain the ultrafast electron transfer that occurs on light excitation of the bound fluorescein. These structural findings support our concept of using lipocalins as a scaffold for the engineering of so-called "anticalins" directed against prescribed targets as an alternative to recombinant antibody fragments.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12945055}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12945055 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12945055}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Pieris brassicae]]
[[Category: Pieris brassicae]]
[[Category: Protein engineering]]
[[Category: Protein engineering]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:56:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:02:42 2008''

Revision as of 09:02, 28 July 2008

Image:1n0s.png

Template:STRUCTURE 1n0s

ENGINEERED LIPOCALIN FLUA IN COMPLEX WITH FLUORESCEIN

Template:ABSTRACT PUBMED 12945055

About this Structure

1N0S is a Single protein structure of sequence from Pieris brassicae. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region., Korndorfer IP, Beste G, Skerra A, Proteins. 2003 Oct 1;53(1):121-9. PMID:12945055

Page seeded by OCA on Mon Jul 28 12:02:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n0s"
Personal tools