This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.




1ab2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ab2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ab2" /> '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE...)
Line 1: Line 1:
-
[[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==
Line 11: Line 10:
==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==
Line 20: Line 19:
[[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)]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:57:23 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:44 2008''

Revision as of 09:42, 21 February 2008


1ab2

Drag the structure with the mouse to rotate

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL

Contents

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.

Disease

Known diseases associated with this structure: Leukemia, Philadelphia chromosome-positive, resistant to imatinib OMIM:[189980]

About this Structure

1AB2 is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Three-dimensional solution structure of the src homology 2 domain of c-abl., Overduin M, Rios CB, Mayer BJ, Baltimore D, Cowburn D, Cell. 1992 Aug 21;70(4):697-704. PMID:1505033

Page seeded by OCA on Thu Feb 21 11:42:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools