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.


1xm2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xm2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xm2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xm2| PDB=1xm2 | SCENE= }}
{{STRUCTURE_1xm2| PDB=1xm2 | SCENE= }}
-
'''Crystal structure of Human PRL-1'''
+
===Crystal structure of Human PRL-1===
-
==Overview==
+
<!--
-
The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15571731}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15571731 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15571731}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Son, J H.]]
[[Category: Son, J H.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:12:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:30:03 2008''

Revision as of 05:30, 28 July 2008

Image:1xm2.png

Template:STRUCTURE 1xm2

Crystal structure of Human PRL-1

Template:ABSTRACT PUBMED 15571731

About this Structure

1XM2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms., Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, Lim SM, Yoon TS, Ryu SE, J Mol Biol. 2005 Jan 14;345(2):401-13. PMID:15571731

Page seeded by OCA on Mon Jul 28 08:30:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xm2"
Personal tools