1gnf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1gnf |SIZE=350|CAPTION= <scene name='initialview01'>1gnf</scene> | |PDB= 1gnf |SIZE=350|CAPTION= <scene name='initialview01'>1gnf</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnf OCA], [http://www.ebi.ac.uk/pdbsum/1gnf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gnf RCSB]</span> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Kowalski, K.]] | [[Category: Kowalski, K.]] | ||
[[Category: Mackay, J P.]] | [[Category: Mackay, J P.]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
[[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 20:47:33 2008'' | ||
Revision as of 20:47, 30 March 2008
| |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE N-TERMINAL ZINC FINGER OF MURINE GATA-1, NMR, 25 STRUCTURES
OverviewOverview
Zinc fingers (ZnFs) are generally regarded as DNA-binding motifs. However, a number of recent reports have implicated particular ZnFs in the mediation of protein-protein interactions. The N-terminal ZnF of GATA-1 (NF) is one such finger, having been shown to interact with a number of other proteins, including the recently discovered transcriptional co-factor FOG. Here we solve the three-dimensional structure of the NF in solution using multidimensional 1H/15N NMR spectroscopy, and we use 1H/15N spin relaxation measurements to investigate its backbone dynamics. The structure consists of two distorted beta-hairpins and a single alpha-helix, and is similar to that of the C-terminal ZnF of chicken GATA-1. Comparisons of the NF structure with those of other C4-type zinc binding motifs, including hormone receptor and LIM domains, also reveal substantial structural homology. Finally, we use the structure to map the spatial locations of NF residues shown by mutagenesis to be essential for FOG binding, and demonstrate that these residues all lie on a single face of the NF. Notably, this face is well removed from the putative DNA-binding face of the NF, an observation which is suggestive of simultaneous roles for the NF; that is, stabilisation of GATA-1 DNA complexes and recruitment of FOG to GATA-1-controlled promoter regions.
About this StructureAbout this Structure
1GNF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG., Kowalski K, Czolij R, King GF, Crossley M, Mackay JP, J Biomol NMR. 1999 Mar;13(3):249-62. PMID:10212985
Page seeded by OCA on Sun Mar 30 20:47:33 2008