2sem
From Proteopedia
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|PDB= 2sem |SIZE=350|CAPTION= <scene name='initialview01'>2sem</scene>, resolution 2.2Å | |PDB= 2sem |SIZE=350|CAPTION= <scene name='initialview01'>2sem</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=IPG:N-ISOPROPYL+GLYCINE'>IPG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sem OCA], [http://www.ebi.ac.uk/pdbsum/2sem PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2sem RCSB]</span> | ||
}} | }} | ||
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[[Category: Turck, C W.]] | [[Category: Turck, C W.]] | ||
[[Category: Zuckermann, R N.]] | [[Category: Zuckermann, R N.]] | ||
| - | [[Category: ACE]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
[[Category: peptoid]] | [[Category: peptoid]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:52 2008'' |
Revision as of 02:02, 31 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2SEM 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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