1ign

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|PDB= 1ign |SIZE=350|CAPTION= <scene name='initialview01'>1ign</scene>, resolution 2.250&Aring;
|PDB= 1ign |SIZE=350|CAPTION= <scene name='initialview01'>1ign</scene>, resolution 2.250&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= RAP1 DNA BINDING DOMAIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= RAP1 DNA BINDING DOMAIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ign FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ign OCA], [http://www.ebi.ac.uk/pdbsum/1ign PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ign RCSB]</span>
}}
}}
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[[Category: Koenig, P.]]
[[Category: Koenig, P.]]
[[Category: Rhodes, D.]]
[[Category: Rhodes, D.]]
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[[Category: homoeodomain]]
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[[Category: rap1,yeast,telomeres,homoeodomain]]
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[[Category: rap1]]
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[[Category: telomere]]
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[[Category: yeast]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:28 2008''

Revision as of 18:19, 30 March 2008


PDB ID 1ign

Drag the structure with the mouse to rotate
, resolution 2.250Å
Ligands: , , ,
Gene: RAP1 DNA BINDING DOMAIN (Saccharomyces cerevisiae)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE


Overview

Telomeres, the nucleoprotein complexes at the ends of eukaryotic chromosomes, are essential for chromosome stability. In the yeast S. cerevisiae, telomeric DNA is bound in a sequence-specific manner by RAP1, a multifunctional protein also involved in transcriptional regulation. Here we report the crystal structure of the DNA-binding domain of RAP1 in complex with telomeric DNA site at 2.25 A resolution. The protein contains two similar domains that bind DNA in a tandem orientation, recognizing a tandemly repeated DNA sequence. The domains are structurally related to the homeodomain and the proto-oncogene Myb, but show novel features in their DNA-binding mode. A structured linker between the domains and a long C-terminal tail contribute to the binding specificity. This structure provides insight into the recognition of the conserved telomeric DNA sequences by a protein.

About this Structure

1IGN is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA., Konig P, Giraldo R, Chapman L, Rhodes D, Cell. 1996 Apr 5;85(1):125-36. PMID:8620531

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