1h0t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h0t.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1h0t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h0t| PDB=1h0t | SCENE= }}
{{STRUCTURE_1h0t| PDB=1h0t | SCENE= }}
-
'''AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING'''
+
===AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING===
-
==Overview==
+
<!--
-
Combinatorial protein engineering provides powerful means for functional selection of novel binding proteins. One class of engineered binding proteins, denoted affibodies, is based on the three-helix scaffold of the Z domain derived from staphylococcal protein A. The Z(SPA-1) affibody has been selected from a phage-displayed library as a binder to protein A. Z(SPA-1) also binds with micromolar affinity to its own ancestor, the Z domain. We have characterized the Z(SPA-1) affibody in its uncomplexed state and determined the solution structure of a Z:Z(SPA-1) protein-protein complex. Uncomplexed Z(SPA-1) behaves as an aggregation-prone molten globule, but folding occurs on binding, and the original (Z) three-helix bundle scaffold is fully formed in the complex. The structural basis for selection and strong binding is a large interaction interface with tight steric and polar/nonpolar complementarity that directly involves 10 of 13 mutated amino acid residues on Z(SPA-1). We also note similarities in how the surface of the Z domain responds by induced fit to binding of Z(SPA-1) and Ig Fc, respectively, suggesting that the Z(SPA-1) affibody is capable of mimicking the morphology of the natural binding partner for the Z domain.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12594333}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12594333 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12594333}}
==About this Structure==
==About this Structure==
-
1H0T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0T OCA].
+
1H0T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0T OCA].
==Reference==
==Reference==
Line 40: Line 44:
[[Category: Protein engineering]]
[[Category: Protein engineering]]
[[Category: Protein-protein interaction]]
[[Category: Protein-protein interaction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:16:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:25:54 2008''

Revision as of 03:25, 1 July 2008

Template:STRUCTURE 1h0t

AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED FOLDING

Template:ABSTRACT PUBMED 12594333

About this Structure

1H0T is a Single protein structure of sequence from Staphylococcus aureus. Full experimental information is available from OCA.

Reference

An affibody in complex with a target protein: structure and coupled folding., Wahlberg E, Lendel C, Helgstrand M, Allard P, Dincbas-Renqvist V, Hedqvist A, Berglund H, Nygren PA, Hard T, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3185-90. Epub 2003 Feb 19. PMID:12594333

Page seeded by OCA on Tue Jul 1 06:25:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools