We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

195d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:195d.gif|left|200px]]
+
{{Seed}}
 +
[[Image:195d.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_195d| PDB=195d | SCENE= }}
{{STRUCTURE_195d| PDB=195d | SCENE= }}
-
'''X-RAY STRUCTURES OF THE B-DNA DODECAMER D(CGCGTTAACGCG) WITH AN INVERTED CENTRAL TETRANUCLEOTIDE AND ITS NETROPSIN COMPLEX'''
+
===X-RAY STRUCTURES OF THE B-DNA DODECAMER D(CGCGTTAACGCG) WITH AN INVERTED CENTRAL TETRANUCLEOTIDE AND ITS NETROPSIN COMPLEX===
-
==Overview==
+
<!--
-
The crystal structures of the B-DNA dodecamer d(CGCGTTAACGCG) duplex (T2A2), with the inverted tetranucleotide core from the duplex d(CGCGAATTCGCG) [A2T2, Dickerson &amp; Drew (1981). J. Mol. Biol. 149, 761-768], and its netropsin complex (T2A2-N) have been determined at 2.3 A resolution. The crystals are orthorhombic, space group P2(1)2(1)2(1), unit-cell dimensions of a = 25.7, b = 40.5 and c = 67.0 A, for T2A2 and a = 25.49, b = 40.87, c = 67.02 A for T2A2-N and are isomorphous with A2T2. The native T2A2 structure, with 70 water molecules had a final R value of 0.15 for 1522 reflections (F &gt; 2sigma), while for the netropsin complex, with 87 water molecules, the R value was 0.16 for 2420 reflections. In T2A2, a discontinuous string of zig-zagging water molecules hydrate the narrow A.T minor groove. In T2A2-N, netropsin binds in one orientation in the minor groove, covering the TTAA central region, by displacing the string of waters, forming the majority of hydrogen bonds with DNA atoms in one strand, and causing very little perturbation of the native structure. The helical twist angle in T2A2 is largest at the duplex center, corresponding to the cleavage site by the restriction enzymes HpaI and HincII. The sequence inversion AATT--&gt;TTAA of the tetranucleotide at the center of the molecule results in a different path for the local helix axis in T2A2 and A2T2 but the overall bending is similar in both cases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299320}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299320 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299320}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Complexed with drug]]
[[Category: Complexed with drug]]
[[Category: Double helix]]
[[Category: Double helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:35:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:40:12 2008''

Revision as of 12:40, 30 June 2008

Image:195d.png

Template:STRUCTURE 195d

X-RAY STRUCTURES OF THE B-DNA DODECAMER D(CGCGTTAACGCG) WITH AN INVERTED CENTRAL TETRANUCLEOTIDE AND ITS NETROPSIN COMPLEX

Template:ABSTRACT PUBMED 15299320

About this Structure

Full crystallographic information is available from OCA.

Reference

X-ray structures of the B-DNA dodecamer d(CGCGTTAACGCG) with an inverted central tetranucleotide and its netropsin complex., Balendiran K, Rao ST, Sekharudu CY, Zon G, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):190-8. PMID:15299320

Page seeded by OCA on Mon Jun 30 15:40:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/195d"
Personal tools