1n0r: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1n0r.gif|left|200px]]
{{Seed}}
[[Image:1n0r.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n0r|  PDB=1n0r  |  SCENE=  }}  
{{STRUCTURE_1n0r|  PDB=1n0r  |  SCENE=  }}  


'''4ANK: A designed ankyrin repeat protein with four identical consensus repeats'''
===4ANK: A designed ankyrin repeat protein with four identical consensus repeats===




==Overview==
<!--
The ankyrin repeat is one of the most common, modular, protein-protein interaction motifs in nature. To understand the structural determinants of this family of proteins and extract the consensus information that defines the architecture of this motif, we have designed a series of idealized ankyrin repeat proteins containing one, two, three, or four repeats by using statistical analysis of approximately 4,000 ankyrin repeat sequences from the PFAM database. Biophysical and x-ray crystallographic studies of the three and four repeat constructs (3ANK and 4ANK) to 1.26 and 1.5 A resolution, respectively, demonstrate that these proteins are well-folded, monomeric, display high thermostability, and adopt a very regular, tightly packed ankyrin repeat fold. Mapping the degree of amino acid conservation at each position on the 4ANK structure shows that most nonconserved residues are clustered on the surface of the molecule that has been designated as the binding site in naturally occurring ankyrin repeat proteins. Thus, the consensus amino acid sequence contains all information required to define the ankyrin repeat fold. Our results suggest that statistical analysis and the consensus sequence approach can be used as an effective method to design proteins with complex topologies. These generic ankyrin repeat proteins can serve as prototypes for dissecting the rules of molecular recognition mediated by ankyrin repeats and for engineering proteins with novel biological functions.
The line below this paragraph, {{ABSTRACT_PUBMED_12461176}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12461176 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12461176}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Ank]]
[[Category: Ank]]
[[Category: Ankyrin repeat]]
[[Category: Ankyrin repeat]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:56:38 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:24:31 2008''

Revision as of 09:24, 27 July 2008

File:1n0r.png


Drag the structure with the mouse to rotate
1n0r, resolution 1.50Å (default scene)
Ligands: BR
Related: 1n0q
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



4ANK: A designed ankyrin repeat protein with four identical consensus repeats

Template:ABSTRACT PUBMED 12461176

About this Structure

Full crystallographic information is available from OCA.

Reference

Consensus-derived structural determinants of the ankyrin repeat motif., Mosavi LK, Minor DL Jr, Peng ZY, Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16029-34. Epub 2002 Dec 2. PMID:12461176

Page seeded by OCA on Sun Jul 27 12:24:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1n0r&oldid=645850"