1el2
From Proteopedia
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|PDB= 1el2 |SIZE=350|CAPTION= <scene name='initialview01'>1el2</scene> | |PDB= 1el2 |SIZE=350|CAPTION= <scene name='initialview01'>1el2</scene> | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=5CM:5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=DU:2'-DEOXYURIDINE-5'-MONOPHOSPHATE'>DU</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1eln|1ELN]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1el2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el2 OCA], [http://www.ebi.ac.uk/pdbsum/1el2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1el2 RCSB]</span> | ||
}} | }} | ||
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[[Category: telomere]] | [[Category: telomere]] | ||
- | ''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 20:04:46 2008'' |
Revision as of 17:04, 30 March 2008
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Ligands: | , , , , | ||||||
Related: | 1ELN
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
SOLUTION STRUCTURE OF A MODIFIED HUMAN TELOMERE FRAGMENT (STRUCTURE "A")
Overview
We present the solution structure of d(CCCTA2CCCTA2CCCTA2CCCT), a fragment of the vertebrate telomere which folds intramolecularly. The four cytidine stretches form an i-motif which includes six intercalated C.C+ pairs and terminates with the cytidines at the 5' extremity of each stretch. Above, the second TA2 linker loops across one of the narrow grooves, while at the bottom, the first and third linkers loop across the wide grooves. At 30 degrees C, the spectra of the first and third linkers are quasi-degenerate. Severe broadening at lower temperature indicates that this results from motional averaging between at least two structures of each bottom loop, and makes it impossible to solve the configuration of the bottom loops directly, in contrast to the rest of the structure. We therefore turned to the modified sequence d(CCCTA(2)5MCCCTA2CCCUA2CCCT) in which the two base substitutions (underlined) break the quasi-symmetry between linkers 1 and 3. The three loops follow approximately the hairpin "second pattern" of Hilbers. In the first loop, T4 is in the syn orientation, whereas its analog in the third loop, U16, oriented anti, is in a central location, where it interacts with bases of both loops, thus contributing to their tight association. The only motion is a syn/anti flip of A18 in the third loop. Returning to the telomere fragment, we show that each of the bottom loops switches between the structures identified in the first and third loops of the modified structure. The motions are concerted, and the resulting configurations of the bottom loop cluster present a bulge to either right (T4 syn) or left (T16 syn).
About this Structure
1EL2 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The solution structure and internal motions of a fragment of the cytidine-rich strand of the human telomere., Phan AT, Gueron M, Leroy JL, J Mol Biol. 2000 May 26;299(1):123-44. PMID:10860727
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