2drp: Difference between revisions
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|PDB= 2drp |SIZE=350|CAPTION= <scene name='initialview01'>2drp</scene>, resolution 2.800Å | |PDB= 2drp |SIZE=350|CAPTION= <scene name='initialview01'>2drp</scene>, resolution 2.800Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <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=2drp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2drp OCA], [http://www.ebi.ac.uk/pdbsum/2drp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2drp RCSB]</span> | |||
}} | }} | ||
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[[Category: Rhodes, D.]] | [[Category: Rhodes, D.]] | ||
[[Category: Schwabe, J W.R.]] | [[Category: Schwabe, J W.R.]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''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 02:38:32 2008'' | ||
Revision as of 02:38, 31 March 2008
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| , resolution 2.800Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION
OverviewOverview
The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived.
About this StructureAbout this Structure
2DRP is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition., Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D, Nature. 1993 Dec 2;366(6454):483-7. PMID:8247159
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