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.


1i07

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i07.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1i07.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i07| PDB=1i07 | SCENE= }}
{{STRUCTURE_1i07| PDB=1i07 | SCENE= }}
-
'''EPS8 SH3 DOMAIN INTERTWINED DIMER'''
+
===EPS8 SH3 DOMAIN INTERTWINED DIMER===
-
==Overview==
+
<!--
-
The SH3 domain of Eps8 was previously found to form an intertwined, domain-swapped dimer. We report here a monomeric structure of the EPS8 SH3 domain obtained from crystals grown at low pH, as well as an improved domain-swapped dimer structure at 1.8 A resolution. In the domain-swapped dimer the asymmetric unit contains two "hybrid-monomers." In the low pH form there are two independently folded SH3 molecules per asymmetric unit. The formation of intermolecular salt bridges is thought to be the reason for the formation of the dimer. On the basis of the monomer SH3 structure, it is argued that Eps8 SH3 should, in principle, bind to peptides containing a PxxP motif. Recently it was reported that Eps8 SH3 binds to a peptide with a PxxDY motif. Because the "SH3 fold" is conserved, alternate binding sites may be possible for the PxxDY motif to bind. The strand exchange or domain swap occurs at the n-src loops because the n-src loops are flexible. The thermal b-factors also indicate the flexible nature of n-src loops and a possible handle for domain swap initiation. Despite the loop swapping, the typical SH3 fold in both forms is conserved structurally. The interface of the acidic form of SH3 is stabilized by a tetragonal network of water molecules above hydrophobic residues. The intertwined dimer interface is stabilized by hydrophobic and aromatic stacking interactions in the core and by hydrophilic interactions on the surface.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11316885}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11316885 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11316885}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Newcomer, M E.]]
[[Category: Newcomer, M E.]]
[[Category: Hormone/growth factor]]
[[Category: Hormone/growth factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:25:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:12:53 2008''

Revision as of 07:12, 1 July 2008

Image:1i07.png

Template:STRUCTURE 1i07

EPS8 SH3 DOMAIN INTERTWINED DIMER

Template:ABSTRACT PUBMED 11316885

About this Structure

1I07 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain., Kishan KV, Newcomer ME, Rhodes TH, Guilliot SD, Protein Sci. 2001 May;10(5):1046-55. PMID:11316885

Page seeded by OCA on Tue Jul 1 10:12:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i07"
Personal tools