2lmr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2lmr.jpg|left|200px]]
+
==Solution structure of the first sam domain of odin==
 +
<StructureSection load='2lmr' size='340' side='right' caption='[[2lmr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 +
== Structural highlights ==
 +
[[2lmr]] is a 1 chain structure with sequence 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=2LMR OCA]. <br>
 +
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
 +
== Publication Abstract from PubMed ==
 +
The EphA2 receptor plays key roles in many physiological and pathological events, including cancer. The process of receptor endocytosis and the consequent degradation have attracted attention as possible means of overcoming the negative outcomes of EphA2 in cancer cells and decreasing tumor malignancy. A recent study indicates that Sam (sterile alpha motif) domains of Odin, a member of the ANKS (ankyrin repeat and sterile alpha motif domain-containing) family of proteins, are important for the regulation of EphA2 endocytosis. Odin contains two tandem Sam domains (Odin-Sam1 and -Sam2). Herein, we report on the nuclear magnetic resonance (NMR) solution structure of Odin-Sam1; through a variety of assays (employing NMR, surface plasmon resonance, and isothermal titration calorimetry techniques), we clearly demonstrate that Odin-Sam1 binds to the Sam domain of EphA2 in the low micromolar range. NMR chemical shift perturbation experiments and molecular modeling studies point out that the two Sam domains interact with a head-to-tail topology characteristic of several Sam-Sam complexes. This binding mode is similar to that we have previously proposed for the association between the Sam domains of the lipid phosphatase Ship2 and EphA2. This work further validates structural elements relevant for the heterotypic Sam-Sam interactions of EphA2 and provides novel insights for the design of potential therapeutic compounds that can modulate receptor endocytosis.
-
<!--
+
Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor.,Mercurio FA, Marasco D, Pirone L, Pedone EM, Pellecchia M, Leone M Biochemistry. 2012 Mar 13;51(10):2136-45. Epub 2012 Mar 5. PMID:22332920<ref>PMID:22332920</ref>
-
The line below this paragraph, containing "STRUCTURE_2lmr", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_2lmr| PDB=2lmr | SCENE= }}
+
-
===Solution structure of the first sam domain of odin===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
== References ==
-
 
+
<references/>
-
<!--
+
__TOC__
-
The line below this paragraph, {{ABSTRACT_PUBMED_22332920}}, adds the Publication Abstract to the page
+
</StructureSection>
-
(as it appears on PubMed at http://www.pubmed.gov), where 22332920 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_22332920}}
+
-
 
+
-
==About this Structure==
+
-
[[2lmr]] is a 1 chain structure with sequence 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=2LMR OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022332920</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Leone, M.]]
[[Category: Leone, M.]]
[[Category: Mercurio, F.]]
[[Category: Mercurio, F.]]
[[Category: Signaling protein]]
[[Category: Signaling protein]]

Revision as of 08:35, 30 April 2014

Solution structure of the first sam domain of odin

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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