This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1shd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1shd.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1shd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1shd| PDB=1shd | SCENE= }}
{{STRUCTURE_1shd| PDB=1shd | SCENE= }}
-
'''PEPTIDE INHIBITORS OF SRC SH3-SH2-PHOSPHOPROTEIN INTERACTIONS'''
+
===PEPTIDE INHIBITORS OF SRC SH3-SH2-PHOSPHOPROTEIN INTERACTIONS===
-
==Overview==
+
<!--
-
Activated pp60c-src has been implicated in a number of human malignancies including colon carcinoma and breast adenocarcinoma. Association of the src SH2 domain with tyrosine-phosphorylated proteins plays a role in src-mediated signal transduction. Inhibitors of src SH2 domain-phosphoprotein interactions are, thus, of great interest in defining the role(s) of src in signal transduction pathways. To facilitate such studies, an enzyme-linked immunosorbent assay (ELISA) was developed to detect inhibitors of src SH2-phosphoprotein interactions. This assay measures inhibition of binding of a fusion construct (glutathione S-transferase src SH3-SH2) with autophosphorylated epidermal growth factor receptor tyrosine kinase domain. Activities of phosphopeptide segments derived from potential src SH2 cognate phosphoprotein partners were determined, with the focal adhesion kinase-derived segment VSETDDY*AEIIDE yielding the highest inhibitory activity. Structure activity studies starting from acetyl (Ac)-Y*EEIE have identified Ac-Y*Y*Y*IE as the most active compound screened in the ELISA. This compound is at least 20-fold more active than the parent peptide Ac-Y*EEIE. A high resolution (2 A) crystal structure of human src SH2 complexed with Ac-Y*EEIE was obtained and provided a useful framework for understanding the structure-activity relationships. Additionally, Ac-Y*EEIE was able to block interactions between src and its cellular phosphoprotein partners in vanadate-treated cell lysates from MDA-MB-468 breast carcinoma cells. However, it is unable to abrogate proliferation of MDA-MB-468 cells in culture, presumably because of poor cell penetration and/or lability of the phosphate group on tyrosine.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7527393}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7527393 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7527393}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Gilmer, T.]]
[[Category: Gilmer, T.]]
[[Category: Jordan, S.]]
[[Category: Jordan, S.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:42:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:11:39 2008''

Revision as of 16:11, 27 July 2008

Image:1shd.png

Template:STRUCTURE 1shd

PEPTIDE INHIBITORS OF SRC SH3-SH2-PHOSPHOPROTEIN INTERACTIONS

Template:ABSTRACT PUBMED 7527393

About this Structure

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

Reference

Peptide inhibitors of src SH3-SH2-phosphoprotein interactions., Gilmer T, Rodriguez M, Jordan S, Crosby R, Alligood K, Green M, Kimery M, Wagner C, Kinder D, Charifson P, et al., J Biol Chem. 1994 Dec 16;269(50):31711-9. PMID:7527393

Page seeded by OCA on Sun Jul 27 19:11:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1shd"
Personal tools