1ley: Difference between revisions

Revision as of 14:44, 21 February 2008

STRUCTURE OF A DICATIONIC MONOIMIDAZOLE LEXITROPSIN BOUND TO DNA (ORIENTATION 2)

OverviewOverview

An X-ray crystal structure has been solved of the complex of a dicationic lexitropsin with a B-DNA duplex of sequence CGCGAATTCGCG. The lexitropsin is identical to netropsin except for replacement of the first methylpyrrole ring by methylimidazole, converting a =CH- to =N-. Crystals are isomorphous with those of the DNA dodecamer in the absence of drug. Although the =N- for =CH- substitution was intended to make that locus on the drug molecule compatible with a G.C base pair, electrostatic attraction for the two cationic ends of the drug predominates, and this lexitropsin binds to the same central AATT site as does the parent netropsin. But unlike netropsin, this lexitropsin exhibits end-for-end disorder in the crystal. Both orientations were refined separately to completion. Final residual errors at 2.25 A resolution for the 2358 reflections above 2 sigma in F are R = 0.165 for one orientation (LexA) with 37 water molecules and 0.164 for the inverted drug orientation (LexB) with 40 water molecules. This molecular disorder is probably attributable to a weakening of binding to the AATT site occasioned by the imidazole-for-pyrrole substitution.

About this StructureAbout this Structure

1LEY is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a dicationic monoimidazole lexitropsin bound to DNA., Goodsell DS, Ng HL, Kopka ML, Lown JW, Dickerson RE, Biochemistry. 1995 Dec 26;34(51):16654-61. PMID:8527438

Page seeded by OCA on Thu Feb 21 13:44:21 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ley.gif|left|200px]]<br /><applet load="1ley" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ley.gif|left|200px]]<br /><applet load="1ley" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ley, resolution 2.250&Aring;" />
 '''STRUCTURE OF A DICATIONIC MONOIMIDAZOLE LEXITROPSIN BOUND TO DNA (ORIENTATION 2)'''<br />
 ==Overview==
-An X-ray crystal structure has been solved of the complex of a dicationic, lexitropsin with a B-DNA duplex of sequence CGCGAATTCGCG. The lexitropsin, is identical to netropsin except for replacement of the first, methylpyrrole ring by methylimidazole, converting a =CH- to =N-. Crystals, are isomorphous with those of the DNA dodecamer in the absence of drug., Although the =N- for =CH- substitution was intended to make that locus on, the drug molecule compatible with a G.C base pair, electrostatic, attraction for the two cationic ends of the drug predominates, and this, lexitropsin binds to the same central AATT site as does the parent, netropsin. But unlike netropsin, this lexitropsin exhibits end-for-end, disorder in the crystal. Both orientations were refined separately to, completion. Final residual errors at 2.25 A resolution for the 2358, reflections above 2 sigma in F are R = 0.165 for one orientation (LexA), with 37 water molecules and 0.164 for the inverted drug orientation (LexB), with 40 water molecules. This molecular disorder is probably attributable, to a weakening of binding to the AATT site occasioned by the, imidazole-for-pyrrole substitution.
+An X-ray crystal structure has been solved of the complex of a dicationic lexitropsin with a B-DNA duplex of sequence CGCGAATTCGCG. The lexitropsin is identical to netropsin except for replacement of the first methylpyrrole ring by methylimidazole, converting a =CH- to =N-. Crystals are isomorphous with those of the DNA dodecamer in the absence of drug. Although the =N- for =CH- substitution was intended to make that locus on the drug molecule compatible with a G.C base pair, electrostatic attraction for the two cationic ends of the drug predominates, and this lexitropsin binds to the same central AATT site as does the parent netropsin. But unlike netropsin, this lexitropsin exhibits end-for-end disorder in the crystal. Both orientations were refined separately to completion. Final residual errors at 2.25 A resolution for the 2358 reflections above 2 sigma in F are R = 0.165 for one orientation (LexA) with 37 water molecules and 0.164 for the inverted drug orientation (LexB) with 40 water molecules. This molecular disorder is probably attributable to a weakening of binding to the AATT site occasioned by the imidazole-for-pyrrole substitution.
 ==About this Structure==
-LEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ILT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LEY OCA].
+LEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ILT:'>ILT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LEY OCA].
 ==Reference==
 Structure of a dicationic monoimidazole lexitropsin bound to DNA., Goodsell DS, Ng HL, Kopka ML, Lown JW, Dickerson RE, Biochemistry. 1995 Dec 26;34(51):16654-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8527438 8527438]
 [[Category: Protein complex]]
-[[Category: Dickerson, R.E.]]
+[[Category: Dickerson, R E.]]
-[[Category: Goodsell, D.S.]]
+[[Category: Goodsell, D S.]]
-[[Category: Kopka, M.L.]]
+[[Category: Kopka, M L.]]
-[[Category: Lown, J.W.]]
+[[Category: Lown, J W.]]
-[[Category: Ng, H.L.]]
+[[Category: Ng, H L.]]
 [[Category: ILT]]
 [[Category: b-dna]]
@@ Line 22: / Line 22: @@
 [[Category: double helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:53:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:21 2008''