1a0n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a0n.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a0n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a0n| PDB=1a0n | SCENE= }}
{{STRUCTURE_1a0n| PDB=1a0n | SCENE= }}
-
'''NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES'''
+
===NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES===
-
==Overview==
+
<!--
-
The interaction of the Fyn SH3 domain with the p85 subunit of PI3-kinase is investigated using structural detail and thermodynamic data. The solution structure complex of the SH3 domain with a proline-rich peptide mimic of the binding site on the p85 subunit is described. This indicates that the peptide binds as a poly(L-proline) type II helix. Circular dichroism spectroscopic studies reveal that in the unbound state the peptide exhibits no structure. Thermodynamic data for the binding of this peptide to the SH3 domain suggest that the weak binding (approximately 31 microM) of this interaction is, in part, due to the entropically unfavorable effect of helix formation (delta S0 = -78 J.mol-1.K-1). Binding of the SH3 domain to the intact p85 subunit (minus its own SH3 domain) is tighter, and the entropic and enthalpic contributions are very different from those given by the peptide interaction (delta S0 = +252 J.mol-1.K-1; delta H0 = +44 kJ.mol-1). From these dramatically different thermodynamic measurements we are able to conclude that the interaction of the proline-rich peptide does not effectively mimic the interaction of the intact p85 subunit with the SH3 domain and suggest that other interactions could be important.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8961927}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8961927 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8961927}}
==About this Structure==
==About this Structure==
-
1A0N is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0N OCA].
+
1A0N is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0N OCA].
==Reference==
==Reference==
Line 34: Line 38:
[[Category: Polyproline-binding]]
[[Category: Polyproline-binding]]
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:38:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:44:26 2008''

Revision as of 12:44, 30 June 2008

Template:STRUCTURE 1a0n

NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES

Template:ABSTRACT PUBMED 8961927

About this Structure

1A0N is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

Reference

Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase., Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE, Biochemistry. 1996 Dec 10;35(49):15646-53. PMID:8961927

Page seeded by OCA on Mon Jun 30 15:44:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools