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.


1u2h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u2h.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1u2h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u2h| PDB=1u2h | SCENE= }}
{{STRUCTURE_1u2h| PDB=1u2h | SCENE= }}
-
'''X-ray Structure of the N-terminally truncated human APEP-1'''
+
===X-ray Structure of the N-terminally truncated human APEP-1===
-
==Overview==
+
<!--
-
BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16354304}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16354304 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16354304}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Rgd motif]]
[[Category: Rgd motif]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:40:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:57:21 2008''

Revision as of 21:57, 5 July 2008

Image:1u2h.png

Template:STRUCTURE 1u2h

X-ray Structure of the N-terminally truncated human APEP-1

Template:ABSTRACT PUBMED 16354304

About this Structure

1U2H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray structure of engineered human Aortic Preferentially Expressed Protein-1 (APEG-1)., Manjasetty BA, Niesen FH, Scheich C, Roske Y, Goetz F, Behlke J, Sievert V, Heinemann U, Bussow K, BMC Struct Biol. 2005 Dec 14;5:21. PMID:16354304

Page seeded by OCA on Sun Jul 6 00:57:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u2h"
Personal tools