1pqn
From Proteopedia
(New page: 200px<br /> <applet load="1pqn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pqn" /> '''dominant negative human hDim1 (hDim1 1-128)...) |
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'''dominant negative human hDim1 (hDim1 1-128)'''<br /> | '''dominant negative human hDim1 (hDim1 1-128)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 142 amino acid Dim1p protein is a component of the U4/U6.U5 tri-snRNP | + | The 142 amino acid Dim1p protein is a component of the U4/U6.U5 tri-snRNP complex required for pre-mRNA splicing and interacts with multiple splicing-associated proteins. To gain further insight into the structural basis of its function, we determined the solution structure of the reduced form of the dominant negative human hDim1 (hDim1(1)(-)(128)) using multidimensional NMR spectroscopy. This dominant negative hDim1 assumes a thioredoxin-like fold, confirming previous NMR and crystallographic results. However, in contrast to a recent crystal structure, the NMR solution structure for the reduced form of hDim1(1)(-)(128) presented here, along with thermodynamic data, indicates that the presence of a disulfide bond between Cys38 and Cys79 is structurally and functionally unimportant. Comparison of the truncated hDim1(1)(-)(128) with the full-length protein, using NMR and circular dichroism spectroscopy, indicates that the 14 C-terminal residues can undergo a local unfolding transition and assume alternative conformations, which appear to play a functional role. Other residues essential for hDim1 function are identified by using mutational and genetic approaches. The residues thus identified are not identical with those previously shown to govern Dim1 interaction with defined protein partners. |
==About this Structure== | ==About this Structure== | ||
| - | 1PQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1PQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cheng, H.]] | [[Category: Cheng, H.]] | ||
| - | [[Category: Golemis, E | + | [[Category: Golemis, E A.]] |
| - | [[Category: Gould, K | + | [[Category: Gould, K L.]] |
[[Category: Roder, H.]] | [[Category: Roder, H.]] | ||
| - | [[Category: Zhang, Y | + | [[Category: Zhang, Y Z.]] |
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
[[Category: cleavage]] | [[Category: cleavage]] | ||
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[[Category: u5-15k spliceosomal protein]] | [[Category: u5-15k spliceosomal protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:33 2008'' |
Revision as of 12:31, 21 February 2008
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dominant negative human hDim1 (hDim1 1-128)
Overview
The 142 amino acid Dim1p protein is a component of the U4/U6.U5 tri-snRNP complex required for pre-mRNA splicing and interacts with multiple splicing-associated proteins. To gain further insight into the structural basis of its function, we determined the solution structure of the reduced form of the dominant negative human hDim1 (hDim1(1)(-)(128)) using multidimensional NMR spectroscopy. This dominant negative hDim1 assumes a thioredoxin-like fold, confirming previous NMR and crystallographic results. However, in contrast to a recent crystal structure, the NMR solution structure for the reduced form of hDim1(1)(-)(128) presented here, along with thermodynamic data, indicates that the presence of a disulfide bond between Cys38 and Cys79 is structurally and functionally unimportant. Comparison of the truncated hDim1(1)(-)(128) with the full-length protein, using NMR and circular dichroism spectroscopy, indicates that the 14 C-terminal residues can undergo a local unfolding transition and assume alternative conformations, which appear to play a functional role. Other residues essential for hDim1 function are identified by using mutational and genetic approaches. The residues thus identified are not identical with those previously shown to govern Dim1 interaction with defined protein partners.
About this Structure
1PQN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis., Zhang YZ, Cheng H, Gould KL, Golemis EA, Roder H, Biochemistry. 2003 Aug 19;42(32):9609-18. PMID:12911302
Page seeded by OCA on Thu Feb 21 14:31:33 2008
