1mdg

From Proteopedia

Revision as of 01:59, 25 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1mdg, resolution 1.50Å

Drag the structure with the mouse to rotate

An Alternating Antiparallel Octaplex in an RNA Crystal Structure

Overview

Multistranded helical structures in nucleic acids play various functions, in biological processes. Here we report the crystal structure of a, hexamer, rU(BrdG)r(AGGU),at 1.5 A resolution containing a structural, complex of an alternating antiparallel eight-stranded helical fragment, that is sandwiched in two tetraplexes. The octaplex is formed by groove, binding interaction and base tetrad intercalation between two tetraplexes., Two different forms of octaplexes have been proposed, which display, different properties in interaction with proteins and nucleic acids., Adenines form a base tetrad in the novel N6-H em leader N3 conformation, and further interact with uridines to form an adenine-uridine octad in the, reverse Hoogsteen pairing scheme. The conformational flexibility of, adenine tetrad indicates that it can optimize its conformation in, different interactions.

About this Structure

1MDG is a Protein complex structure of sequences from [1] with NA and NCO as ligands. Full crystallographic information is available from OCA.

Reference

An eight-stranded helical fragment in RNA crystal structure: implications for tetraplex interaction., Pan B, Xiong Y, Shi K, Sundaralingam M, Structure. 2003 Jul;11(7):825-31. PMID:12842045

Page seeded by OCA on Sun Nov 25 04:07:08 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools