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New page: left|200px<br /> <applet load="1ab2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ab2" /> '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE...
 
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[[Image:1ab2.gif|left|200px]]<br />
[[Image:1ab2.gif|left|200px]]<br /><applet load="1ab2" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ab2" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ab2" />
caption="1ab2" />
'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL'''<br />
'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL'''<br />


==Overview==
==Overview==
SH2 regions are protein motifs capable of binding target protein sequences, that contain a phosphotyrosine. The solution structure of the abl SH2, product, a protein of 109 residues and 12.1 kd, has been determined by, multidimensional nuclear magnetic resonance spectroscopy. It is a compact, spherical domain with a pair of three-stranded antiparallel beta sheets, and a C-terminal alpha helix enclosing the hydrophobic core. Three, arginines project from a short N-terminal alpha helix and one beta sheet, into the putative phosphotyrosine-binding site, which lies on a face, distal from the termini. Comparison with other SH2 sequences supports a, common global fold and mode of phosphotyrosine binding for this family.
SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine. The solution structure of the abl SH2 product, a protein of 109 residues and 12.1 kd, has been determined by multidimensional nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a pair of three-stranded antiparallel beta sheets and a C-terminal alpha helix enclosing the hydrophobic core. Three arginines project from a short N-terminal alpha helix and one beta sheet into the putative phosphotyrosine-binding site, which lies on a face distal from the termini. Comparison with other SH2 sequences supports a common global fold and mode of phosphotyrosine binding for this family.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1AB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AB2 OCA].  
1AB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB2 OCA].  


==Reference==
==Reference==
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[[Category: Baltimore, D.]]
[[Category: Baltimore, D.]]
[[Category: Cowburn, D.]]
[[Category: Cowburn, D.]]
[[Category: Mayer, B.J.]]
[[Category: Mayer, B J.]]
[[Category: Overduin, M.]]
[[Category: Overduin, M.]]
[[Category: Rios, C.B.]]
[[Category: Rios, C B.]]
[[Category: transferase(phosphotransferase)]]
[[Category: transferase(phosphotransferase)]]


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