1hsq: Difference between revisions

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==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.

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==

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[[Category: phosphoric diester hydrolase]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 20: / Line 20: @@
 [[Category: phosphoric diester hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:27 2008''