1wo5
From Proteopedia
(New page: 200px<br /> <applet load="1wo5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wo5" /> '''Solution structure of Designed Functional F...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1wo5.gif|left|200px]]<br /> | + | [[Image:1wo5.gif|left|200px]]<br /><applet load="1wo5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1wo5" size=" | + | |
caption="1wo5" /> | caption="1wo5" /> | ||
'''Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain'''<br /> | '''Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Zinc binding motifs have received much attention in the area of protein | + | Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1WO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http:// | + | 1WO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WO5 OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Crossley, M.]] | [[Category: Crossley, M.]] | ||
| - | [[Category: Liew, C | + | [[Category: Liew, C K.]] |
| - | [[Category: Mackay, J | + | [[Category: Mackay, J P.]] |
| - | [[Category: Matthews, J | + | [[Category: Matthews, J M.]] |
| - | [[Category: Sharpe, B | + | [[Category: Sharpe, B K.]] |
| - | [[Category: Wilce, J | + | [[Category: Wilce, J A.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:26 2008'' |
Revision as of 13:46, 21 February 2008
|
Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain
Contents |
Overview
Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates.
Disease
Known diseases associated with this structure: Blue-cone monochromacy OMIM:[303900], Colorblindness, protan OMIM:[303900], Rubenstein-Taybi syndrome OMIM:[600140]
About this Structure
1WO5 is a Single protein structure of sequence from [1] with as ligand. Active as Histone acetyltransferase, with EC number 2.3.1.48 Full crystallographic information is available from OCA.
Reference
Assessment of the robustness of a serendipitous zinc binding fold: mutagenesis and protein grafting., Sharpe BK, Liew CK, Kwan AH, Wilce JA, Crossley M, Matthews JM, Mackay JP, Structure. 2005 Feb;13(2):257-66. PMID:15698569
Page seeded by OCA on Thu Feb 21 15:46:26 2008
