1b07: Difference between revisions

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~~'''~~CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR~~'''~~

===CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9851931}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9851931 is the PubMed ID number.

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==About this Structure==

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[[Category: Sh3 domain]]

[[Category: Signal transduction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:54:25 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:57:51 2008''

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-[[Image:1b07.gif|left|200px]]
+{{Seed}}
+[[Image:1b07.png|left|200px]]
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 {{STRUCTURE_1b07|  PDB=1b07  |  SCENE=  }}
-'''CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9851931}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9851931 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9851931}}
 ==About this Structure==
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 [[Category: Sh3 domain]]
 [[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:54:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:57:51 2008''