1msz: Difference between revisions

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[[Image:1msz.gif|left|200px]]
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[[Image:1msz.png|left|200px]]


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{{STRUCTURE_1msz|  PDB=1msz  |  SCENE=  }}  
{{STRUCTURE_1msz|  PDB=1msz  |  SCENE=  }}  


'''Solution structure of the R3H domain from human Smubp-2'''
===Solution structure of the R3H domain from human Smubp-2===




==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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==About this Structure==
==About this Structure==
1MSZ is a [[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].  
1MSZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MSZ OCA].  


==Reference==
==Reference==
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[[Category: Sharipo, A.]]
[[Category: Sharipo, A.]]
[[Category: R3h fold]]
[[Category: R3h fold]]
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