1kyj

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(New page: 200px<br /><applet load="1kyj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kyj" /> '''Tumor Associated Mucin Motif from CD43 prote...)
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[[Image:1kyj.gif|left|200px]]<br /><applet load="1kyj" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Tumor Associated Mucin Motif from CD43 protein'''<br />
'''Tumor Associated Mucin Motif from CD43 protein'''<br />
==Overview==
==Overview==
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The structural characteristics of a mucin glycopeptide motif derived from, the N-terminal fragment STTAV of the cell surface glycoprotein CD43 have, been investigated by NMR. In this study, a series of molecules prepared by, total synthesis were examined, consisting of the peptide itself, three, glycopeptides having clustered sites of alpha-O-glycosylation on the, serine and threonine side chains with the Tn, TF, and STF carbohydrate, antigens, respectively, and one with the beta-O-linked TF antigen., Additionally, a glycopeptide having the sequence SSSAVAV, triglycosylated, with the Le(y) epitope, was investigated. NMR data for the tri-STF-STTAV, glycopeptide were used to solve the structure of this construct through, restrained molecular dynamics calculations. The calculations revealed a, defined conformation for the glycopeptide core rooted in the interaction, of the peptide and the first N-acetylgalactosamine residue. The similarity, of the NMR data for each of the alpha-O-linked glycopeptides demonstrates, that this structure persists for each construct and that the mode of, attachment of the first sugar and the peptide is paramount in establishing, the organization of the core. The core provides a common framework on, which a variety of glycans may be displayed. Remarkably, while there is a, profound organizational effect on the peptide backbone with the, alpha-linked glycans, attachment via a beta-linkage has little apparent, consequence.
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The structural characteristics of a mucin glycopeptide motif derived from the N-terminal fragment STTAV of the cell surface glycoprotein CD43 have been investigated by NMR. In this study, a series of molecules prepared by total synthesis were examined, consisting of the peptide itself, three glycopeptides having clustered sites of alpha-O-glycosylation on the serine and threonine side chains with the Tn, TF, and STF carbohydrate antigens, respectively, and one with the beta-O-linked TF antigen. Additionally, a glycopeptide having the sequence SSSAVAV, triglycosylated with the Le(y) epitope, was investigated. NMR data for the tri-STF-STTAV glycopeptide were used to solve the structure of this construct through restrained molecular dynamics calculations. The calculations revealed a defined conformation for the glycopeptide core rooted in the interaction of the peptide and the first N-acetylgalactosamine residue. The similarity of the NMR data for each of the alpha-O-linked glycopeptides demonstrates that this structure persists for each construct and that the mode of attachment of the first sugar and the peptide is paramount in establishing the organization of the core. The core provides a common framework on which a variety of glycans may be displayed. Remarkably, while there is a profound organizational effect on the peptide backbone with the alpha-linked glycans, attachment via a beta-linkage has little apparent consequence.
==About this Structure==
==About this Structure==
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1KYJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with A2G and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1SIA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KYJ OCA].
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1KYJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=A2G:'>A2G</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1SIA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYJ OCA].
==Reference==
==Reference==
Principles of mucin architecture: structural studies on synthetic glycopeptides bearing clustered mono-, di-, tri-, and hexasaccharide glycodomains., Coltart DM, Royyuru AK, Williams LJ, Glunz PW, Sames D, Kuduk SD, Schwarz JB, Chen XT, Danishefsky SJ, Live DH, J Am Chem Soc. 2002 Aug 21;124(33):9833-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12175243 12175243]
Principles of mucin architecture: structural studies on synthetic glycopeptides bearing clustered mono-, di-, tri-, and hexasaccharide glycodomains., Coltart DM, Royyuru AK, Williams LJ, Glunz PW, Sames D, Kuduk SD, Schwarz JB, Chen XT, Danishefsky SJ, Live DH, J Am Chem Soc. 2002 Aug 21;124(33):9833-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12175243 12175243]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chen, X.T.]]
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[[Category: Chen, X T.]]
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[[Category: Coltart, D.M.]]
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[[Category: Coltart, D M.]]
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[[Category: Danishefsky, S.D.]]
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[[Category: Danishefsky, S D.]]
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[[Category: Glunz, P.W.]]
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[[Category: Glunz, P W.]]
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[[Category: Kuduk, S.D.]]
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[[Category: Kuduk, S D.]]
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[[Category: Live, D.H.]]
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[[Category: Live, D H.]]
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[[Category: Royyuru, A.K.]]
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[[Category: Royyuru, A K.]]
[[Category: Sames, D.]]
[[Category: Sames, D.]]
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[[Category: Schwarz, J.B.]]
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[[Category: Schwarz, J B.]]
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[[Category: Williams, L.J.]]
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[[Category: Williams, L J.]]
[[Category: A2G]]
[[Category: A2G]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: mucin glycoprotein]]
[[Category: mucin glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:11:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:19 2008''

Revision as of 11:39, 21 February 2008


1kyj

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Tumor Associated Mucin Motif from CD43 protein

Overview

The structural characteristics of a mucin glycopeptide motif derived from the N-terminal fragment STTAV of the cell surface glycoprotein CD43 have been investigated by NMR. In this study, a series of molecules prepared by total synthesis were examined, consisting of the peptide itself, three glycopeptides having clustered sites of alpha-O-glycosylation on the serine and threonine side chains with the Tn, TF, and STF carbohydrate antigens, respectively, and one with the beta-O-linked TF antigen. Additionally, a glycopeptide having the sequence SSSAVAV, triglycosylated with the Le(y) epitope, was investigated. NMR data for the tri-STF-STTAV glycopeptide were used to solve the structure of this construct through restrained molecular dynamics calculations. The calculations revealed a defined conformation for the glycopeptide core rooted in the interaction of the peptide and the first N-acetylgalactosamine residue. The similarity of the NMR data for each of the alpha-O-linked glycopeptides demonstrates that this structure persists for each construct and that the mode of attachment of the first sugar and the peptide is paramount in establishing the organization of the core. The core provides a common framework on which a variety of glycans may be displayed. Remarkably, while there is a profound organizational effect on the peptide backbone with the alpha-linked glycans, attachment via a beta-linkage has little apparent consequence.

About this Structure

1KYJ is a Protein complex structure of sequences from [1] with and as ligands. This structure supersedes the now removed PDB entry 1SIA. Full crystallographic information is available from OCA.

Reference

Principles of mucin architecture: structural studies on synthetic glycopeptides bearing clustered mono-, di-, tri-, and hexasaccharide glycodomains., Coltart DM, Royyuru AK, Williams LJ, Glunz PW, Sames D, Kuduk SD, Schwarz JB, Chen XT, Danishefsky SJ, Live DH, J Am Chem Soc. 2002 Aug 21;124(33):9833-44. PMID:12175243

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