1hsq
From Proteopedia
(New page: 200px<br /> <applet load="1hsq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hsq" /> '''SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHO...) |
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'''SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA'''<br /> | '''SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HSQ 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/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] Full crystallographic information is available from [http:// | + | 1HSQ 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/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phosphoric diester hydrolase]] | [[Category: phosphoric diester hydrolase]] | ||
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Revision as of 13:57, 15 February 2008
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SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA
Overview
SH3 (Src homology 3) domains are found in many signaling proteins and, appear to function as binding modules for cytoplasmic target proteins. The, solution structure of the SH3 domain of human phospholipase C-gamma, (PLC-gamma) was determined by two-dimensional 1H NMR analysis. This SH3, domain is composed of eight antiparallel beta strands consisting of two, successive "Greek key" motifs, which form a barrel-like structure. The, conserved aliphatic and aromatic residues form a hydrophobic pocket on the, molecular surface, and the conserved carboxylic residues are localized to, the periphery. The hydrophobic pocket may serve as a binding site for, target proteins. Analysis of the slowly exchanging amide protons by NMR, measurements indicates that despite containing a high content of beta, structure, the SH3 domain of PLC-gamma is flexible.
About this Structure
1HSQ is a Single protein structure of sequence from Homo sapiens. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 Full crystallographic information is available from OCA.
Reference
Solution structure of the SH3 domain of phospholipase C-gamma., Kohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J, Inagaki F, Cell. 1993 Mar 26;72(6):953-60. PMID:7681365
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