1bhh: Difference between revisions

Revision as of 19:10, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bhh.png

Template:STRUCTURE 1bhh

FREE P56LCK SH2 DOMAINFREE P56LCK SH2 DOMAIN

Template:ABSTRACT PUBMED 9685372

About this StructureAbout this Structure

1BHH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding., Tong L, Warren TC, Lukas S, Schembri-King J, Betageri R, Proudfoot JR, Jakes S, J Biol Chem. 1998 Aug 7;273(32):20238-42. PMID:9685372

Page seeded by OCA on Mon Jun 30 19:10:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bhh.jpg|left|200px]]
+{{Seed}}
+[[Image:1bhh.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bhh|  PDB=1bhh  |  SCENE=  }}
-'''FREE P56LCK SH2 DOMAIN'''
+===FREE P56LCK SH2 DOMAIN===
-==Overview==
+<!--
-The crystal structure of human p56(lck) SH2 domain in complex with an inhibitor containing the singly charged p-(carboxymethyl)phenylalanine residue (cmF) as a phosphotyrosine (Tyr(P) or pY) replacement has been determined at 1.8 A resolution. The binding mode of the acetyl-cmF-Glu-Glu-Ile (cmFEEI) inhibitor is very similar to that of the pYEEI inhibitor, confirming that the cmFEEI inhibitor has a similar mechanism of SH2 domain inhibition despite its significantly reduced potency. Observed conformational differences in the side chain of the cmF residue can be interpreted in terms of maintaining similar interactions with the SH2 domain as the Tyr(P) residue. The crystal structure of the free p56(lck) SH2 domain has been determined at 1.9 A resolution and shows an open conformation for the BC loop and an open phosphotyrosine binding pocket, in contrast to earlier studies on the src SH2 domain that showed mostly closed conformation. The structural information presented here suggests that the carboxymethyl-phenylalanine residue may be a viable Tyr(P) replacement and represents an attractive starting point for the design and development of SH2 domain inhibitors with better pharmaceutical profiles.
+The line below this paragraph, {{ABSTRACT_PUBMED_9685372}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9685372 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9685372}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Sh2 domain]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:31:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:32 2008''