1cit

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(New page: 200px<br /><applet load="1cit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cit, resolution 2.7&Aring;" /> '''DNA-BINDING MECHANISM...)
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'''DNA-BINDING MECHANISM OF THE MONOMERIC ORPHAN NUCLEAR RECEPTOR NGFI-B'''<br />
'''DNA-BINDING MECHANISM OF THE MONOMERIC ORPHAN NUCLEAR RECEPTOR NGFI-B'''<br />
==Overview==
==Overview==
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The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the, orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed, to its high-affinity DNA target, represents the first structure analysis, of a nuclear receptor DBD bound as a monomer to DNA. The structure of the, core DBD and its interactions with the major groove of the DNA are similar, to previously crystallographically solved DBD-DNA complexes in this, superfamily; however, residues C-terminal to this core form a separate and, unique substructure that interacts extensively and in a sequence-specific, way with the minor groove of its DNA target, in particular with the, characteristic 3 A-T base-pair identity element that extends 5' to the, usual nuclear receptor half-site (AGGTCA).
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The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed to its high-affinity DNA target, represents the first structure analysis of a nuclear receptor DBD bound as a monomer to DNA. The structure of the core DBD and its interactions with the major groove of the DNA are similar to previously crystallographically solved DBD-DNA complexes in this superfamily; however, residues C-terminal to this core form a separate and unique substructure that interacts extensively and in a sequence-specific way with the minor groove of its DNA target, in particular with the characteristic 3 A-T base-pair identity element that extends 5' to the usual nuclear receptor half-site (AGGTCA).
==About this Structure==
==About this Structure==
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1CIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CIT OCA].
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1CIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIT OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Meinke, G.]]
[[Category: Meinke, G.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: early immediate response gene product]]
[[Category: early immediate response gene product]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:29:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:35 2008''

Revision as of 10:06, 21 February 2008


1cit, resolution 2.7Å

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DNA-BINDING MECHANISM OF THE MONOMERIC ORPHAN NUCLEAR RECEPTOR NGFI-B

Overview

The 2.7 A X-ray crystal structure of the DNA-binding domain (DBD) of the orphan nuclear receptor, nerve growth factor-induced-B (NGFI-B), complexed to its high-affinity DNA target, represents the first structure analysis of a nuclear receptor DBD bound as a monomer to DNA. The structure of the core DBD and its interactions with the major groove of the DNA are similar to previously crystallographically solved DBD-DNA complexes in this superfamily; however, residues C-terminal to this core form a separate and unique substructure that interacts extensively and in a sequence-specific way with the minor groove of its DNA target, in particular with the characteristic 3 A-T base-pair identity element that extends 5' to the usual nuclear receptor half-site (AGGTCA).

About this Structure

1CIT is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B., Meinke G, Sigler PB, Nat Struct Biol. 1999 May;6(5):471-7. PMID:10331876

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