2sem: Difference between revisions

Line 1:

[[Image:2sem.~~jpg~~|left|200px]]

[[Image:2sem.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR~~'''~~

===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.~~

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.

-->

==About this Structure==

Line 33:

Line 37:

[[Category: Sh3 domain]]

[[Category: Signal transduction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 17~~:18:00 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:21:24 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2sem.jpg|left|200px]]
+{{Seed}}
+[[Image:2sem.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2sem|  PDB=2sem  |  SCENE=  }}
-'''SEM5 SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR'''
+===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.
+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==
@@ Line 33: / Line 37: @@
 [[Category: Sh3 domain]]
 [[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:18:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:21:24 2008''