1gfc: Difference between revisions

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[[Image:1gfc.gif|left|200px]]<br />

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

<applet load="1gfc" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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'''SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE C-TERMINAL SH3 DOMAIN OF GRB2'''<br />

==Overview==

BACKGROUND: Growth factor receptor-bound protein 2 (GRB2) is an adaptor, protein with three Src homology (SH) domains in the order SH3-SH2-SH3., Both SH3 domains of GRB2 are necessary for interaction with the protein, Son of sevenless (Sos), which acts as a Ras activator. Thus, GRB2 mediates, signal transduction from growth factor receptors to Ras and is thought to, be a key molecule in signal transduction. RESULTS: The three-dimensional, structure of the carboxy-terminal SH3 domain of GRB2 (GRB2 C-SH3) was, determined by NMR spectroscopy. The SH3 structure consists of six, beta-strands arranged in two beta-sheets that are packed together, perpendicularly with two additional beta-strands forming the third, beta-sheet. GRB2 C-SH3 is very similar to SH3 domains from other proteins., The binding site of the ligand peptide (VPP-PVPPRRR) derived from the Sos, protein was mapped on the GRB2 C-SH3 domain indirectly using 1H and 15N, chemical shift changes, and directly using several intermolecular nuclear, Overhauser effects. CONCLUSIONS: Despite the structural similarity among, the known SH3 domains, the sequence alignment and the secondary structure, assignments differ. We therefore propose a standard description of the SH3, structures to facilitate comparison of individual SH3 domains, based on, their three-dimensional structures. The binding site of the ligand peptide, on GRB2 C-SH3 is in good agreement with those found in other SH3 domains.

BACKGROUND: Growth factor receptor-bound protein 2 (GRB2) is an adaptor protein with three Src homology (SH) domains in the order SH3-SH2-SH3. Both SH3 domains of GRB2 are necessary for interaction with the protein Son of sevenless (Sos), which acts as a Ras activator. Thus, GRB2 mediates signal transduction from growth factor receptors to Ras and is thought to be a key molecule in signal transduction. RESULTS: The three-dimensional structure of the carboxy-terminal SH3 domain of GRB2 (GRB2 C-SH3) was determined by NMR spectroscopy. The SH3 structure consists of six beta-strands arranged in two beta-sheets that are packed together perpendicularly with two additional beta-strands forming the third beta-sheet. GRB2 C-SH3 is very similar to SH3 domains from other proteins. The binding site of the ligand peptide (VPP-PVPPRRR) derived from the Sos protein was mapped on the GRB2 C-SH3 domain indirectly using 1H and 15N chemical shift changes, and directly using several intermolecular nuclear Overhauser effects. CONCLUSIONS: Despite the structural similarity among the known SH3 domains, the sequence alignment and the secondary structure assignments differ. We therefore propose a standard description of the SH3 structures to facilitate comparison of individual SH3 domains, based on their three-dimensional structures. The binding site of the ligand peptide on GRB2 C-SH3 is in good agreement with those found in other SH3 domains.

==Disease==

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==About this Structure==

1GFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1GFC OCA].

1GFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GFC OCA].

==Reference==

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[[Category: adaptor protein containing sh2 and sh3]]

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-[[Image:1gfc.gif|left|200px]]<br />
+[[Image:1gfc.gif|left|200px]]<br /><applet load="1gfc" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1gfc" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1gfc" />
 '''SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE C-TERMINAL SH3 DOMAIN OF GRB2'''<br />
 ==Overview==
-BACKGROUND: Growth factor receptor-bound protein 2 (GRB2) is an adaptor, protein with three Src homology (SH) domains in the order SH3-SH2-SH3., Both SH3 domains of GRB2 are necessary for interaction with the protein, Son of sevenless (Sos), which acts as a Ras activator. Thus, GRB2 mediates, signal transduction from growth factor receptors to Ras and is thought to, be a key molecule in signal transduction. RESULTS: The three-dimensional, structure of the carboxy-terminal SH3 domain of GRB2 (GRB2 C-SH3) was, determined by NMR spectroscopy. The SH3 structure consists of six, beta-strands arranged in two beta-sheets that are packed together, perpendicularly with two additional beta-strands forming the third, beta-sheet. GRB2 C-SH3 is very similar to SH3 domains from other proteins., The binding site of the ligand peptide (VPP-PVPPRRR) derived from the Sos, protein was mapped on the GRB2 C-SH3 domain indirectly using 1H and 15N, chemical shift changes, and directly using several intermolecular nuclear, Overhauser effects. CONCLUSIONS: Despite the structural similarity among, the known SH3 domains, the sequence alignment and the secondary structure, assignments differ. We therefore propose a standard description of the SH3, structures to facilitate comparison of individual SH3 domains, based on, their three-dimensional structures. The binding site of the ligand peptide, on GRB2 C-SH3 is in good agreement with those found in other SH3 domains.
+BACKGROUND: Growth factor receptor-bound protein 2 (GRB2) is an adaptor protein with three Src homology (SH) domains in the order SH3-SH2-SH3. Both SH3 domains of GRB2 are necessary for interaction with the protein Son of sevenless (Sos), which acts as a Ras activator. Thus, GRB2 mediates signal transduction from growth factor receptors to Ras and is thought to be a key molecule in signal transduction. RESULTS: The three-dimensional structure of the carboxy-terminal SH3 domain of GRB2 (GRB2 C-SH3) was determined by NMR spectroscopy. The SH3 structure consists of six beta-strands arranged in two beta-sheets that are packed together perpendicularly with two additional beta-strands forming the third beta-sheet. GRB2 C-SH3 is very similar to SH3 domains from other proteins. The binding site of the ligand peptide (VPP-PVPPRRR) derived from the Sos protein was mapped on the GRB2 C-SH3 domain indirectly using 1H and 15N chemical shift changes, and directly using several intermolecular nuclear Overhauser effects. CONCLUSIONS: Despite the structural similarity among the known SH3 domains, the sequence alignment and the secondary structure assignments differ. We therefore propose a standard description of the SH3 structures to facilitate comparison of individual SH3 domains, based on their three-dimensional structures. The binding site of the ligand peptide on GRB2 C-SH3 is in good agreement with those found in other SH3 domains.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-GFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GFC OCA].
+GFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GFC OCA].
 ==Reference==
@@ Line 23: / Line 22: @@
 [[Category: adaptor protein containing sh2 and sh3]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:04:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:25 2008''