1n0r
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1n0r |SIZE=350|CAPTION= <scene name='initialview01'>1n0r</scene>, resolution 1.50Å | |PDB= 1n0r |SIZE=350|CAPTION= <scene name='initialview01'>1n0r</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene> | + | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1n0q|1N0Q]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0r OCA], [http://www.ebi.ac.uk/pdbsum/1n0r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n0r RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Mosavi, L K.]] | [[Category: Mosavi, L K.]] | ||
[[Category: Peng, Z-Y.]] | [[Category: Peng, Z-Y.]] | ||
| - | [[Category: BR]] | ||
[[Category: ank]] | [[Category: ank]] | ||
[[Category: ankyrin repeat]] | [[Category: ankyrin repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:43 2008'' |
Revision as of 19:23, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1N0Q
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1N0R is a Protein complex structure of sequences from [1]. 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 [[Category: ]]
Page seeded by OCA on Sun Mar 30 22:23:43 2008
