1mm2
From Proteopedia
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|PDB= 1mm2 |SIZE=350|CAPTION= <scene name='initialview01'>1mm2</scene> | |PDB= 1mm2 |SIZE=350|CAPTION= <scene name='initialview01'>1mm2</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fp0|1FP0]], [[1f62|1f62]], [[1mm3|1MM3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm2 OCA], [http://www.ebi.ac.uk/pdbsum/1mm2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mm2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Matthews, J M.]] | [[Category: Matthews, J M.]] | ||
[[Category: Verger, A.]] | [[Category: Verger, A.]] | ||
| - | [[Category: ZN]] | ||
[[Category: phd]] | [[Category: phd]] | ||
[[Category: protein scaffold]] | [[Category: protein scaffold]] | ||
[[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 Sun Mar 30 22:17:52 2008'' |
Revision as of 19:17, 30 March 2008
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| Ligands: | |||||||
| Gene: | CHD4 (Homo sapiens) | ||||||
| Related: | 1FP0, 1f62, 1MM3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the 2nd PHD domain from Mi2b
Overview
The design of proteins with tailored functions remains a relatively elusive goal. Small size, a well-defined structure, and the ability to maintain structural integrity despite multiple mutations are all desirable properties for such designer proteins. Many zinc binding domains fit this description. We determined the structure of a PHD finger from the transcriptional cofactor Mi2beta and investigated the suitability of this domain as a scaffold for presenting selected binding functions. The two flexible loops in the structure were mutated extensively by either substitution or expansion, without affecting the overall fold of the domain. A binding site for the corepressor CtBP2 was also grafted onto the domain, creating a new PHD domain that can specifically bind CtBP2 both in vitro and in the context of a eukaryotic cell nucleus. These results represent a step toward designing new regulatory proteins for modulating aberrant gene expression in vivo.
About this Structure
1MM2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Engineering a protein scaffold from a PHD finger., Kwan AH, Gell DA, Verger A, Crossley M, Matthews JM, Mackay JP, Structure. 2003 Jul;11(7):803-13. PMID:12842043
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