1wo5
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1wo5 |SIZE=350|CAPTION= <scene name='initialview01'>1wo5</scene> | |PDB= 1wo5 |SIZE=350|CAPTION= <scene name='initialview01'>1wo5</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1liq|1LIQ]], [[1wo3|1WO3]], [[1wo4|1WO4]], [[1wo6|1WO6]], [[1wo7|1WO7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wo5 OCA], [http://www.ebi.ac.uk/pdbsum/1wo5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wo5 RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=303900 303900]], Colorblindness, protan OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=303900 303900]], Rubenstein-Taybi syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600140 600140]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 31: | Line 31: | ||
[[Category: Sharpe, B K.]] | [[Category: Sharpe, B K.]] | ||
[[Category: Wilce, J A.]] | [[Category: Wilce, J A.]] | ||
| - | [[Category: ZN]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:38:53 2008'' |
Revision as of 21:38, 30 March 2008
| |||||||
| Ligands: | |||||||
| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 | ||||||
| Related: | 1LIQ, 1WO3, 1WO4, 1WO6, 1WO7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of Designed Functional Finger 2 (DFF2): Designed mutant based on non-native CHANCE domain
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.
About this Structure
1WO5 is a Single protein structure of sequence from [1]. 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 Mon Mar 31 00:38:53 2008
