397d
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of an HIV-1 trans-activation response region (TAR) | + | The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-A resolution. In this crystal structure, the characteristic UCU bulge of TAR adopts a conformation that is stabilized by three divalent calcium ions and differs from those determined previously by solution NMR. One metal ion, crucial to the loop conformation, binds directly to three phosphates in the loop region. The structure emphasizes the influence of metal ion binding on RNA structure and, given the abundance of divalent metal ion in the cell, raises the question of whether metal ions play a role in the conformation of TAR RNA and the interaction of TAR with Tat and cyclin T in vivo. |
==About this Structure== | ==About this Structure== | ||
| Line 12: | Line 12: | ||
A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation., Ippolito JA, Steitz TA, Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9819-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9707559 9707559] | A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation., Ippolito JA, Steitz TA, Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9819-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9707559 9707559] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Ippolito, J | + | [[Category: Ippolito, J A.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: overhanging bases]] | [[Category: overhanging bases]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:02:37 2008'' |
Revision as of 17:02, 21 February 2008
|
A 1.3 A RESOLUTION CRYSTAL STRUCTURE OF THE HIV-1 TRANS-ACTIVATION RESPONSE REGION RNA STEM REVEALS A METAL ION-DEPENDENT BULGE CONFORMATION
Overview
The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-A resolution. In this crystal structure, the characteristic UCU bulge of TAR adopts a conformation that is stabilized by three divalent calcium ions and differs from those determined previously by solution NMR. One metal ion, crucial to the loop conformation, binds directly to three phosphates in the loop region. The structure emphasizes the influence of metal ion binding on RNA structure and, given the abundance of divalent metal ion in the cell, raises the question of whether metal ions play a role in the conformation of TAR RNA and the interaction of TAR with Tat and cyclin T in vivo.
About this Structure
397D is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation., Ippolito JA, Steitz TA, Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9819-24. PMID:9707559
Page seeded by OCA on Thu Feb 21 19:02:37 2008
