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2arg

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[[Image:2arg.jpg|left|200px]]
[[Image:2arg.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2arg |SIZE=350|CAPTION= <scene name='initialview01'>2arg</scene>
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The line below this paragraph, containing "STRUCTURE_2arg", 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=ARM:DEOXY-METHYL-ARGININE'>ARM</scene>, <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_2arg| PDB=2arg | 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=2arg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2arg OCA], [http://www.ebi.ac.uk/pdbsum/2arg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2arg RCSB]</span>
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}}
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'''FORMATION OF AN AMINO ACID BINDING POCKET THROUGH ADAPTIVE ZIPPERING-UP OF A LARGE DNA HAIRPIN LOOP, NMR, 9 STRUCTURES'''
'''FORMATION OF AN AMINO ACID BINDING POCKET THROUGH ADAPTIVE ZIPPERING-UP OF A LARGE DNA HAIRPIN LOOP, NMR, 9 STRUCTURES'''
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==About this Structure==
==About this Structure==
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2ARG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARG OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARG OCA].
==Reference==
==Reference==
Formation of an amino-acid-binding pocket through adaptive zippering-up of a large DNA hairpin loop., Lin CH, Wang W, Jones RA, Patel DJ, Chem Biol. 1998 Oct;5(10):555-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9818148 9818148]
Formation of an amino-acid-binding pocket through adaptive zippering-up of a large DNA hairpin loop., Lin CH, Wang W, Jones RA, Patel DJ, Chem Biol. 1998 Oct;5(10):555-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9818148 9818148]
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[[Category: Protein complex]]
 
[[Category: Jones, R A.]]
[[Category: Jones, R A.]]
[[Category: Lin, C H.]]
[[Category: Lin, C H.]]
[[Category: Patel, D J.]]
[[Category: Patel, D J.]]
[[Category: Wang, W.]]
[[Category: Wang, W.]]
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[[Category: adaptive dna structural transition]]
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[[Category: Adaptive dna structural transition]]
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[[Category: base encapsulation within minor groove]]
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[[Category: Base encapsulation within minor groove]]
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[[Category: deoxyribonucleic acid]]
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[[Category: Deoxyribonucleic acid]]
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[[Category: dna aptamer]]
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[[Category: Dna aptamer]]
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[[Category: l-argininamide binding pocket]]
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[[Category: L-argininamide binding pocket]]
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[[Category: minor groove recognition]]
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[[Category: Minor groove recognition]]
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[[Category: molecular recognition of an amino acid]]
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[[Category: Molecular recognition of an amino acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:23:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:18 2008''
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Revision as of 16:23, 3 May 2008

Template:STRUCTURE 2arg

FORMATION OF AN AMINO ACID BINDING POCKET THROUGH ADAPTIVE ZIPPERING-UP OF A LARGE DNA HAIRPIN LOOP, NMR, 9 STRUCTURES


Overview

BACKGROUND: In vitro selection has identified DNA aptamers that target cofactors, amino acids, peptides and proteins. Structure determination of such ligand-DNA aptamer complexes should elucidate the details of adaptive DNA structural transitions, binding-pocket architectures and ligand recognition. We have determined the solution structure of the complex of a DNA aptamer containing a guanine-rich 18-residue hairpin loop that binds L-argininamide with approximately 100 microM affinity. RESULTS: The DNA aptamer generates its L-argininamide-binding pocket by adaptive zippering up the 18-residue loop through formation of Watson-Crick pairs, mismatch pairs and base triples, while maximizing stacking interactions. Three of the four base triples involve minor-groove recognition through sheared G.A mismatch formation. The unique fold is also achieved through positioning of an adenine residue deep within the minor groove and through nestling of a smaller loop within the larger loop on complex formation. The accessibility to the unique L-argininamide-binding pocket is restricted by a base pair that bridges across one side of the major-groove-binding site. The guanidinium group of the bound L-argininamide aligns through intermolecular hydrogen-bond formation with the base edges of nonadjacent guanine and cytosine residues while being sandwiched between the planes of nonadjacent guanine residues. CONCLUSIONS: The available structures of L-arginine/L-argininamide bound to their DNA and RNA targets define the common principles and patterns associated with molecular recognition, as well as the diversity of intermolecular hydrogen-bonding alignments associated with the distinct binding pockets.

About this Structure

Full crystallographic information is available from OCA.

Reference

Formation of an amino-acid-binding pocket through adaptive zippering-up of a large DNA hairpin loop., Lin CH, Wang W, Jones RA, Patel DJ, Chem Biol. 1998 Oct;5(10):555-72. PMID:9818148 Page seeded by OCA on Sat May 3 19:23:08 2008

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