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1msz
From Proteopedia
(New page: 200px<br /> <applet load="1msz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1msz" /> '''Solution structure of the R3H domain from h...) |
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| - | [[Image:1msz.gif|left|200px]]<br /> | + | [[Image:1msz.gif|left|200px]]<br /><applet load="1msz" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of the R3H domain from human Smubp-2'''<br /> | '''Solution structure of the R3H domain from human Smubp-2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The R3H domain is a conserved sequence motif, identified in over 100 | + | The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MSZ 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:// | + | 1MSZ 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=1MSZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: r3h fold]] | [[Category: r3h fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:57 2008'' |
Revision as of 11:58, 21 February 2008
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Solution structure of the R3H domain from human Smubp-2
Contents |
Overview
The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general.
Disease
Known diseases associated with this structure: Neuronopathy, distal hereditary motor, type VI OMIM:[600502]
About this Structure
1MSZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the R3H domain from human Smubp-2., Liepinsh E, Leonchiks A, Sharipo A, Guignard L, Otting G, J Mol Biol. 2003 Feb 7;326(1):217-23. PMID:12547203
Page seeded by OCA on Thu Feb 21 13:58:57 2008
