1n4e

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[[Image:1n4e.gif|left|200px]]
[[Image:1n4e.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1n4e |SIZE=350|CAPTION= <scene name='initialview01'>1n4e</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1n4e", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1n4e| PDB=1n4e | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4e OCA], [http://www.ebi.ac.uk/pdbsum/1n4e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n4e RCSB]</span>
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}}
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'''Crystal Structure of a DNA Decamer Containing a Thymine-dimer'''
'''Crystal Structure of a DNA Decamer Containing a Thymine-dimer'''
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==About this Structure==
==About this Structure==
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1N4E is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. The following page contains interesting information on the relation of 1N4E with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4E OCA].
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The following page contains interesting information on the relation of 1N4E with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4E OCA].
==Reference==
==Reference==
Polymerization of calsequestrin. Implications for Ca2+ regulation., Park H, Wu S, Dunker AK, Kang C, J Biol Chem. 2003 May 2;278(18):16176-82. Epub 2003 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12594204 12594204]
Polymerization of calsequestrin. Implications for Ca2+ regulation., Park H, Wu S, Dunker AK, Kang C, J Biol Chem. 2003 May 2;278(18):16176-82. Epub 2003 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12594204 12594204]
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[[Category: Protein complex]]
 
[[Category: Thymine Dimers]]
[[Category: Thymine Dimers]]
[[Category: Kang, C.]]
[[Category: Kang, C.]]
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[[Category: Taylor, J S.]]
[[Category: Taylor, J S.]]
[[Category: Zhang, K.]]
[[Category: Zhang, K.]]
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[[Category: dna decamer]]
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[[Category: Dna decamer]]
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[[Category: thymine dimer]]
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[[Category: Thymine dimer]]
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[[Category: uv-damaged dna]]
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[[Category: Uv-damaged dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:04:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:16 2008''
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Revision as of 23:04, 2 May 2008

Image:1n4e.gif

Template:STRUCTURE 1n4e

Crystal Structure of a DNA Decamer Containing a Thymine-dimer


Overview

Two distinct dimerization contacts in calsequestrin crystals suggested a mechanism for Ca(2+) regulation resulting from the occurrence of coupled Ca(2+) binding and protein polymerization. Ca(2+)-induced formation of one contact was proposed to lead to dimerization followed by Ca(2+)-induced formation of the second contact to bring about polymerization (). To test this mechanism, we compared canine cardiac calsequestrin and four truncation mutants with regard to their folding properties, structures, and Ca(2+)-induced polymerization. The wild-type calsequestrin and truncation mutants exhibited similar K(+)-induced folding and end-point structures as indicated by intrinsic fluorescence and circular dichroism, respectively, whereas the polymerization tendencies of the wild-type calsequestrin differed markedly from the polymerization tendencies of the truncation mutants. Static laser light scattering and 3,3'-dithiobis sulfosuccinimidyl-propionate cross-linking indicated that wild-type protein exhibited an initial Ca(2+)-induced dimerization, followed by additional oligomerization as the Ca(2+) concentration was raised or as the K(+) concentration was lowered. None of the truncation mutants exhibited clear stepwise oligomerization that depended on increasing Ca(2+) concentration. Comparison of the three-dimensional structure of rabbit skeletal calsequestrin with a homology model of canine cardiac calsequestrin from the point of view of our coupled Ca(2+) binding and polymerization mechanism leads to a possible explanation for the 2-fold reduced Ca(2+) binding capacity of cardiac calsequestrin despite very similar overall net negative charge for the two proteins.

About this Structure

The following page contains interesting information on the relation of 1N4E with [Thymine Dimers]. Full crystallographic information is available from OCA.

Reference

Polymerization of calsequestrin. Implications for Ca2+ regulation., Park H, Wu S, Dunker AK, Kang C, J Biol Chem. 2003 May 2;278(18):16176-82. Epub 2003 Feb 19. PMID:12594204 Page seeded by OCA on Sat May 3 02:04:48 2008

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