1bw5
From Proteopedia
(New page: 200px<br /><applet load="1bw5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bw5" /> '''THE NMR SOLUTION STRUCTURE OF THE HOMEODOMAI...) |
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| - | [[Image:1bw5.gif|left|200px]]<br /><applet load="1bw5" size=" | + | [[Image:1bw5.gif|left|200px]]<br /><applet load="1bw5" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''THE NMR SOLUTION STRUCTURE OF THE HOMEODOMAIN OF THE RAT INSULIN GENE ENHANCER PROTEIN ISL-1, 50 STRUCTURES'''<br /> | '''THE NMR SOLUTION STRUCTURE OF THE HOMEODOMAIN OF THE RAT INSULIN GENE ENHANCER PROTEIN ISL-1, 50 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Homeodomains are one of the key families of eukaryotic DNA-binding motifs | + | Homeodomains are one of the key families of eukaryotic DNA-binding motifs and provide an important model system for DNA recognition. We have determined a high-quality nuclear magnetic resonance (NMR) structure of the DNA-binding homeodomain of the insulin gene enhancer protein Isl-1 (Isl-1-HD). It forms the first solution structure of a homeodomain from the LIM family. It contains a well-defined inner core (residues 12-55) consisting of the classical three-helix structure observed in other homeodomains. The N terminus is unstructured up to residue 8, while the C terminus gradually becomes unstructured from residue 55 onwards. Some flexibility is evident in the loop parts of the inner core. Isl-1-HD has, despite its low sequence identity (23-34 %), a structure that is strikingly similar to that of the other homeodomains with known three-dimensional structures. Detailed analysis of Isl-1-HD and the other homeodomains rationalizes the differences in their temperature stability and explains the low stability of the Isl-1-HD in the free state (tm 22-30 degrees C). Upon DNA binding, a significant stabilization occurs (tm>55 degrees C). The low stability of Isl-1-HD (and other mammalian homeodomains) suggests that in vivo Isl-1-HD recognizes its cognate DNA from its unfolded state. |
==About this Structure== | ==About this Structure== | ||
| - | 1BW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1BW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Behravan, G.]] | [[Category: Behravan, G.]] | ||
| - | [[Category: Ippel, J | + | [[Category: Ippel, J H.]] |
[[Category: Larsson, G.]] | [[Category: Larsson, G.]] | ||
[[Category: Lundqvist, M.]] | [[Category: Lundqvist, M.]] | ||
| - | [[Category: Lycksell, P | + | [[Category: Lycksell, P O.]] |
[[Category: Schleucher, J.]] | [[Category: Schleucher, J.]] | ||
| - | [[Category: Wijmenga, S | + | [[Category: Wijmenga, S S.]] |
[[Category: Zdunek, J.]] | [[Category: Zdunek, J.]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
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[[Category: lim domain]] | [[Category: lim domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:41 2008'' |
Revision as of 09:59, 21 February 2008
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THE NMR SOLUTION STRUCTURE OF THE HOMEODOMAIN OF THE RAT INSULIN GENE ENHANCER PROTEIN ISL-1, 50 STRUCTURES
Overview
Homeodomains are one of the key families of eukaryotic DNA-binding motifs and provide an important model system for DNA recognition. We have determined a high-quality nuclear magnetic resonance (NMR) structure of the DNA-binding homeodomain of the insulin gene enhancer protein Isl-1 (Isl-1-HD). It forms the first solution structure of a homeodomain from the LIM family. It contains a well-defined inner core (residues 12-55) consisting of the classical three-helix structure observed in other homeodomains. The N terminus is unstructured up to residue 8, while the C terminus gradually becomes unstructured from residue 55 onwards. Some flexibility is evident in the loop parts of the inner core. Isl-1-HD has, despite its low sequence identity (23-34 %), a structure that is strikingly similar to that of the other homeodomains with known three-dimensional structures. Detailed analysis of Isl-1-HD and the other homeodomains rationalizes the differences in their temperature stability and explains the low stability of the Isl-1-HD in the free state (tm 22-30 degrees C). Upon DNA binding, a significant stabilization occurs (tm>55 degrees C). The low stability of Isl-1-HD (and other mammalian homeodomains) suggests that in vivo Isl-1-HD recognizes its cognate DNA from its unfolded state.
About this Structure
1BW5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomains., Ippel H, Larsson G, Behravan G, Zdunek J, Lundqvist M, Schleucher J, Lycksell PO, Wijmenga S, J Mol Biol. 1999 May 14;288(4):689-703. PMID:10329173
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