3sem: Difference between revisions
New page: left|200px<br /><applet load="3sem" size="450" color="white" frame="true" align="right" spinBox="true" caption="3sem, resolution 2.2Å" /> '''SEM5 SH3 DOMAIN COMPL... |
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[[Image:3sem.jpg|left|200px]]<br /><applet load="3sem" size=" | [[Image:3sem.jpg|left|200px]]<br /><applet load="3sem" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="3sem, resolution 2.2Å" /> | caption="3sem, resolution 2.2Å" /> | ||
'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''<br /> | '''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''<br /> | ||
==Overview== | ==Overview== | ||
Src homology 3 (SH3) and WW protein interaction domains bind specific | 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== | ||
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:// | 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]] | ||
[[Category: Cohen, F | [[Category: Cohen, F E.]] | ||
[[Category: Lim, W | [[Category: Lim, W A.]] | ||
[[Category: Nguyen, J | [[Category: Nguyen, J T.]] | ||
[[Category: Turck, C | [[Category: Turck, C W.]] | ||
[[Category: Zuckermann, R | [[Category: Zuckermann, R N.]] | ||
[[Category: inhibitors]] | [[Category: inhibitors]] | ||
[[Category: peptoids]] | [[Category: peptoids]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http:// | ''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
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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
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