1h8c

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(New page: 200px<br /> <applet load="1h8c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h8c" /> '''UBX DOMAIN FROM HUMAN FAF1'''<br /> ==Over...)
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'''UBX DOMAIN FROM HUMAN FAF1'''<br />
'''UBX DOMAIN FROM HUMAN FAF1'''<br />
==Overview==
==Overview==
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The UBX domain is an 80 amino acid residue module that is present, typically at the carboxyl terminus of a variety of eukaryotic proteins. In, an effort to elucidate the function of UBX domains, we solved the, three-dimensional structure of the UBX domain of human Fas-associated, factor-1 (FAF1) by NMR spectroscopy. The structure has a beta-Grasp fold, characterised by a beta-beta-alpha-beta-beta-alpha-beta, secondary-structure organisation. The five beta strands are arranged into, a mixed sheet in the order 21534. The longer first helix packs across the, first three strands of the sheet, and a second shorter 3(10) helix is, located in an extended loop connecting strands 4 and 5. In the absence of, significant sequence similarity, the UBX domain can be superimposed with, ubiquitin with an r.m.s.d. of 1.9 A, suggesting that the two structures, share the same superfold, and an evolutionary relationship. However, the, absence of a carboxyl-terminal extension containing a double glycine motif, and of suitably positioned lysine side-chains makes it highly unlikely, that UBX domains are either conjugated to other proteins or part of mixed, UBX-ubiquitin chains. Database searches revealed that most UBX, domain-containing proteins belong to one of four evolutionarily conserved, families represented by the human FAF1, p47, Y33K, and Rep8 proteins. A, role of the UBX domain in ubiquitin-related processes is suggested.
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The UBX domain is an 80 amino acid residue module that is present typically at the carboxyl terminus of a variety of eukaryotic proteins. In an effort to elucidate the function of UBX domains, we solved the three-dimensional structure of the UBX domain of human Fas-associated factor-1 (FAF1) by NMR spectroscopy. The structure has a beta-Grasp fold characterised by a beta-beta-alpha-beta-beta-alpha-beta secondary-structure organisation. The five beta strands are arranged into a mixed sheet in the order 21534. The longer first helix packs across the first three strands of the sheet, and a second shorter 3(10) helix is located in an extended loop connecting strands 4 and 5. In the absence of significant sequence similarity, the UBX domain can be superimposed with ubiquitin with an r.m.s.d. of 1.9 A, suggesting that the two structures share the same superfold, and an evolutionary relationship. However, the absence of a carboxyl-terminal extension containing a double glycine motif and of suitably positioned lysine side-chains makes it highly unlikely that UBX domains are either conjugated to other proteins or part of mixed UBX-ubiquitin chains. Database searches revealed that most UBX domain-containing proteins belong to one of four evolutionarily conserved families represented by the human FAF1, p47, Y33K, and Rep8 proteins. A role of the UBX domain in ubiquitin-related processes is suggested.
==About this Structure==
==About this Structure==
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1H8C 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=1H8C OCA].
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1H8C 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=1H8C OCA].
==Reference==
==Reference==
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[[Category: faf1 ubx domain ubiquitin-like]]
[[Category: faf1 ubx domain ubiquitin-like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:13:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:33 2008''

Revision as of 10:58, 21 February 2008


1h8c

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UBX DOMAIN FROM HUMAN FAF1

Overview

The UBX domain is an 80 amino acid residue module that is present typically at the carboxyl terminus of a variety of eukaryotic proteins. In an effort to elucidate the function of UBX domains, we solved the three-dimensional structure of the UBX domain of human Fas-associated factor-1 (FAF1) by NMR spectroscopy. The structure has a beta-Grasp fold characterised by a beta-beta-alpha-beta-beta-alpha-beta secondary-structure organisation. The five beta strands are arranged into a mixed sheet in the order 21534. The longer first helix packs across the first three strands of the sheet, and a second shorter 3(10) helix is located in an extended loop connecting strands 4 and 5. In the absence of significant sequence similarity, the UBX domain can be superimposed with ubiquitin with an r.m.s.d. of 1.9 A, suggesting that the two structures share the same superfold, and an evolutionary relationship. However, the absence of a carboxyl-terminal extension containing a double glycine motif and of suitably positioned lysine side-chains makes it highly unlikely that UBX domains are either conjugated to other proteins or part of mixed UBX-ubiquitin chains. Database searches revealed that most UBX domain-containing proteins belong to one of four evolutionarily conserved families represented by the human FAF1, p47, Y33K, and Rep8 proteins. A role of the UBX domain in ubiquitin-related processes is suggested.

About this Structure

1H8C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The UBX domain: a widespread ubiquitin-like module., Buchberger A, Howard MJ, Proctor M, Bycroft M, J Mol Biol. 2001 Mar 16;307(1):17-24. PMID:11243799

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