1b07
From Proteopedia
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| - | [[Image:1b07.gif|left|200px]] | + | [[Image:1b07.gif|left|200px]] |
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| - | '''CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR''' | + | {{Structure |
| + | |PDB= 1b07 |SIZE=350|CAPTION= <scene name='initialview01'>1b07</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PYL:PHENYLETHANE'>PYL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B07 is a [ | + | 1B07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B07 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9851931 9851931] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Zuckermann, R N.]] | [[Category: Zuckermann, R N.]] | ||
[[Category: PYL]] | [[Category: PYL]] | ||
| - | [[Category: | + | [[Category: inhibitor]] |
| - | [[Category: | + | [[Category: peptoid]] |
| - | [[Category: proline-rich | + | [[Category: proline-rich motif]] |
[[Category: protein-protein recognition]] | [[Category: protein-protein recognition]] | ||
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:33 2008'' |
Revision as of 08:04, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRK 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
1B07 is a Single protein structure of sequence from Mus musculus. 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 Mar 20 10:04:33 2008
