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3sem

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(New page: 200px<br /><applet load="3sem" size="450" color="white" frame="true" align="right" spinBox="true" caption="3sem, resolution 2.2&Aring;" /> '''SEM5 SH3 DOMAIN COMPL...)
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[[Image:3sem.jpg|left|200px]]<br /><applet load="3sem" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:3sem.jpg|left|200px]]<br /><applet load="3sem" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3sem, resolution 2.2&Aring;" />
caption="3sem, resolution 2.2&Aring;" />
'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''<br />
'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''<br />
==Overview==
==Overview==
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Src homology 3 (SH3) and WW protein interaction domains bind specific, proline-rich sequences. However, instead of recognizing critical prolines, on the basis of side chain shape or rigidity, these domains broadly, accepted amide N-substituted residues. Proline is apparently specifically, selected in vivo, despite low complementarity, because it is the only, endogenous N-substituted amino acid. This discriminatory mechanism, explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The, mechanism can be exploited: screening a series of ligands in which key, prolines were replaced by nonnatural N-substituted residues yielded a, ligand that selectively bound the Grb2 SH3 domain with 100 times greater, affinity.
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Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity.
==About this Structure==
==About this Structure==
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3SEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3SEM OCA].
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3SEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SEM OCA].
==Reference==
==Reference==
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cohen, F.E.]]
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[[Category: Cohen, F E.]]
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[[Category: Lim, W.A.]]
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[[Category: Lim, W A.]]
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[[Category: Nguyen, J.T.]]
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[[Category: Nguyen, J T.]]
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[[Category: Turck, C.W.]]
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[[Category: Turck, C W.]]
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[[Category: Zuckermann, R.N.]]
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[[Category: Zuckermann, R N.]]
[[Category: inhibitors]]
[[Category: inhibitors]]
[[Category: peptoids]]
[[Category: peptoids]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:58:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:18 2008''

Revision as of 17:11, 21 February 2008


3sem, resolution 2.2Å

Drag the structure with the mouse to rotate

SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR

Overview

Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity.

About this Structure

3SEM is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors., Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA, Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931

Page seeded by OCA on Thu Feb 21 19:11:18 2008

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