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1tce

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(New page: 200px<br /> <applet load="1tce" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tce" /> '''SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAI...)
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'''SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE'''<br />
'''SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE'''<br />
==Overview==
==Overview==
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She is a widely expressed adapter protein that plays an important role in, signaling via a variety of cell surface receptors and has been implicated, in coupling the stimulation of growth factor, cytokine, and antigen, receptors to the Ras signaling pathway. She interacts with several, tyrosine-phosphorylated receptors through its C-terminal SH2 domain, and, one of the mechanisms of T-cell receptor-mediated Ras activation involves, the interaction of the Shc SH2 domain with the tyrosine-phosphorylated, zeta chain of the T-cell receptor. Here we describe a high-resolution NMR, structure of the Shc SH2 domain complexed to a phosphopeptide, (GHDGLpYQGLSTATK) corresponding to a portion of the zeta chain of the, T-cell receptor. Although the overall architecture of the protein is, similar to other SH2 domains, distinct structural differences were, observed in the smaller beta-sheet, BG loop, (pY + 3), phosphopeptide-binding site, and relative position of the bound, phosphopeptide.
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She is a widely expressed adapter protein that plays an important role in signaling via a variety of cell surface receptors and has been implicated in coupling the stimulation of growth factor, cytokine, and antigen receptors to the Ras signaling pathway. She interacts with several tyrosine-phosphorylated receptors through its C-terminal SH2 domain, and one of the mechanisms of T-cell receptor-mediated Ras activation involves the interaction of the Shc SH2 domain with the tyrosine-phosphorylated zeta chain of the T-cell receptor. Here we describe a high-resolution NMR structure of the Shc SH2 domain complexed to a phosphopeptide (GHDGLpYQGLSTATK) corresponding to a portion of the zeta chain of the T-cell receptor. Although the overall architecture of the protein is similar to other SH2 domains, distinct structural differences were observed in the smaller beta-sheet, BG loop, (pY + 3) phosphopeptide-binding site, and relative position of the bound phosphopeptide.
==Disease==
==Disease==
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Known disease associated with this structure: Immunodeficiency due to defect in CD3-zeta OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186780 186780]]
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Known diseases associated with this structure: Immunodeficiency due to defect in CD3-zeta OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186780 186780]]
==About this Structure==
==About this Structure==
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1TCE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TCE OCA].
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1TCE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TCE OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Burakoff, S.J.]]
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[[Category: Burakoff, S J.]]
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[[Category: Feisk, S.W.]]
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[[Category: Feisk, S W.]]
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[[Category: Logan, T.M.]]
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[[Category: Logan, T M.]]
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[[Category: Meadows, R.P.]]
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[[Category: Meadows, R P.]]
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[[Category: Ravichandran, K.S.]]
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[[Category: Ravichandran, K S.]]
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[[Category: Wade, W.R.]]
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[[Category: Wade, W R.]]
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[[Category: Yoon, H.S.]]
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[[Category: Yoon, H S.]]
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[[Category: Zhou, M.M.]]
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[[Category: Zhou, M M.]]
[[Category: complex (signal transduction/peptide)]]
[[Category: complex (signal transduction/peptide)]]
[[Category: sh2 domain]]
[[Category: sh2 domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:23:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:07 2008''

Revision as of 13:12, 21 February 2008


1tce

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SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE

Contents

Overview

She is a widely expressed adapter protein that plays an important role in signaling via a variety of cell surface receptors and has been implicated in coupling the stimulation of growth factor, cytokine, and antigen receptors to the Ras signaling pathway. She interacts with several tyrosine-phosphorylated receptors through its C-terminal SH2 domain, and one of the mechanisms of T-cell receptor-mediated Ras activation involves the interaction of the Shc SH2 domain with the tyrosine-phosphorylated zeta chain of the T-cell receptor. Here we describe a high-resolution NMR structure of the Shc SH2 domain complexed to a phosphopeptide (GHDGLpYQGLSTATK) corresponding to a portion of the zeta chain of the T-cell receptor. Although the overall architecture of the protein is similar to other SH2 domains, distinct structural differences were observed in the smaller beta-sheet, BG loop, (pY + 3) phosphopeptide-binding site, and relative position of the bound phosphopeptide.

Disease

Known diseases associated with this structure: Immunodeficiency due to defect in CD3-zeta OMIM:[186780]

About this Structure

1TCE is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor., Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, Ravichandran KS, Burakoff SJ, Fesik SW, Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7784-8. PMID:7544002

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