1msz

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(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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'''Solution structure of the R3H domain from human Smubp-2'''<br />
'''Solution structure of the R3H domain from human Smubp-2'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MSZ OCA].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:48 2007''
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''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


1msz

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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

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