1sha: Difference between revisions

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[[Image:1sha.gif|left|200px]]<br /><applet load="1sha" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1sha.gif|left|200px]]<br /><applet load="1sha" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1sha, resolution 1.5Å" />

'''CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES'''<br />

==Overview==

Three-dimensional structures of complexes of the SH2 domain of the v-src, oncogene product with two phosphotyrosyl peptides have been determined by, X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A, central antiparallel beta-sheet in the structure is flanked by two, alpha-helices, with peptide binding mediated by the sheet, intervening, loops and one of the helices. The specific recognition of phosphotyrosine, involves amino-aromatic interactions between lysine and arginine side, chains and the ring system in addition to hydrogen-bonding interactions, with the phosphate.

Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.

==About this Structure==

1SHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. 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=1SHA OCA].

1SHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. 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=1SHA OCA].

==Reference==

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[[Category: phosphotransferase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:23:~~13 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:28 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1sha.gif|left|200px]]<br /><applet load="1sha" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sha.gif|left|200px]]<br /><applet load="1sha" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sha, resolution 1.5&Aring;" />
 '''CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES'''<br />
 ==Overview==
-Three-dimensional structures of complexes of the SH2 domain of the v-src, oncogene product with two phosphotyrosyl peptides have been determined by, X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A, central antiparallel beta-sheet in the structure is flanked by two, alpha-helices, with peptide binding mediated by the sheet, intervening, loops and one of the helices. The specific recognition of phosphotyrosine, involves amino-aromatic interactions between lysine and arginine side, chains and the ring system in addition to hydrogen-bonding interactions, with the phosphate.
+Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.
 ==About this Structure==
-SHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. 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=1SHA OCA].
+SHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. 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=1SHA OCA].
 ==Reference==
@@ Line 18: / Line 18: @@
 [[Category: phosphotransferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:23:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:28 2008''