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.


2h5k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h5k.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2h5k.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h5k| PDB=2h5k | SCENE= }}
{{STRUCTURE_2h5k| PDB=2h5k | SCENE= }}
-
'''Crystal Structure of Complex Between the Domain-Swapped Dimeric Grb2 SH2 Domain and Shc-Derived Ligand, Ac-NH-pTyr-Val-Asn-NH2'''
+
===Crystal Structure of Complex Between the Domain-Swapped Dimeric Grb2 SH2 Domain and Shc-Derived Ligand, Ac-NH-pTyr-Val-Asn-NH2===
-
==Overview==
+
<!--
-
The SH2 domain of growth factor receptor-bound protein 2 (Grb2) has been the focus of numerous studies, primarily because of the important roles it plays in signal transduction. More recently, it has emerged as a useful protein to study the consequences of ligand preorganization upon energetics and structure in protein-ligand interactions. The Grb2-SH2 domain is known to form a domain-swapped dimer, and as part of our investigations toward correlating structure and energetics in biological systems, we examined the effects that domain-swapping dimerization of the Grb2-SH2 domain had upon ligand binding affinities. Isothermal titration calorimetry was performed using Grb2-SH2 in both its monomeric and domain-swapped dimeric forms and a phosphorylated tripeptide AcNH-pTyr-Val-Asn-NH(2) that is similar to the Shc sequence recognized by Grb2-SH2 in vivo. The two binding sites of domain-swapped dimer exhibited a 4- and a 13-fold reduction in ligand affinity compared to monomer. Crystal structures of peptide-bound and uncomplexed forms of Grb2-SH2 domain-swapped dimer were obtained and reveal that the orientation of residues V122, V123, and R142 may influence the conformation of W121, an amino acid that is believed to play an important role in Grb2-SH2 ligand sequence specificity. These findings suggest that domain-swapping of Grb2-SH2 not only results in a lower affinity for a Shc-derived ligand, but it may also affect ligand specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17466257}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17466257 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17466257}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Domain-swapping]]
[[Category: Domain-swapping]]
[[Category: Protein-phosphopeptide complex]]
[[Category: Protein-phosphopeptide complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:53:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:48:38 2008''

Revision as of 12:48, 28 July 2008

Image:2h5k.png

Template:STRUCTURE 2h5k

Crystal Structure of Complex Between the Domain-Swapped Dimeric Grb2 SH2 Domain and Shc-Derived Ligand, Ac-NH-pTyr-Val-Asn-NH2

Template:ABSTRACT PUBMED 17466257

About this Structure

2H5K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and energetic aspects of Grb2-SH2 domain-swapping., Benfield AP, Whiddon BB, Clements JH, Martin SF, Arch Biochem Biophys. 2007 Jun 1;462(1):47-53. Epub 2007 Apr 2. PMID:17466257

Page seeded by OCA on Mon Jul 28 15:48:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h5k"
Personal tools