1ab2
From Proteopedia
(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...) |
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'''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 | + | 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:// | + | 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 | + | [[Category: Mayer, B J.]] |
[[Category: Overduin, M.]] | [[Category: Overduin, M.]] | ||
- | [[Category: Rios, C | + | [[Category: Rios, C B.]] |
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
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