We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2oy3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2oy3.gif|left|200px]]<br /><applet load="2oy3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2oy3.gif|left|200px]]
-
caption="2oy3, resolution 1.780&Aring;" />
+
 
-
'''Crystal structure analysis of the monomeric SRCR domain of mouse MARCO'''<br />
+
{{Structure
 +
|PDB= 2oy3 |SIZE=350|CAPTION= <scene name='initialview01'>2oy3</scene>, resolution 1.780&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
 +
|ACTIVITY=
 +
|GENE= Marco ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
 +
}}
 +
 
 +
'''Crystal structure analysis of the monomeric SRCR domain of mouse MARCO'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2OY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OY3 OCA].
+
2OY3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OY3 OCA].
==Reference==
==Reference==
-
Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition., Ojala JR, Pikkarainen T, Tuuttila A, Sandalova T, Tryggvason K, J Biol Chem. 2007 Jun 1;282(22):16654-66. Epub 2007 Apr 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17405873 17405873]
+
Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition., Ojala JR, Pikkarainen T, Tuuttila A, Sandalova T, Tryggvason K, J Biol Chem. 2007 Jun 1;282(22):16654-66. Epub 2007 Apr 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17405873 17405873]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 26: Line 35:
[[Category: scavenger receptor cysteine-rich (srcr)]]
[[Category: scavenger receptor cysteine-rich (srcr)]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:07 2008''

Revision as of 16:06, 20 March 2008


PDB ID 2oy3

Drag the structure with the mouse to rotate
, resolution 1.780Å
Ligands:
Gene: Marco (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



Crystal structure analysis of the monomeric SRCR domain of mouse MARCO


Overview

MARCO is a trimeric class A scavenger receptor of macrophages and dendritic cells that recognizes polyanionic particles and pathogens. The distal, scavenger receptor cysteine-rich (SRCR) domain of the extracellular part of this receptor has been implicated in ligand binding. To provide a structural basis for understanding the ligand-binding mechanisms of MARCO, we have determined the crystal structure of the mouse MARCO SRCR domain. The recombinant SRCR domain purified as monomeric and dimeric forms, and their structures were determined at 1.78 and 1.77 A resolution, respectively. The monomer has a compact globular fold with a twisted five-stranded antiparallel beta-sheet and a long loop covering a single alpha-helix, whereas the dimer is formed via beta-strand swapping of two monomers, thus containing a large eight-stranded beta-sheet. Calculation of the surface electrostatic potential revealed that the beta-sheet region with several arginines forms a basic cluster. Unexpectedly, an acidic cluster was found in the long loop region. In the monomer, the acidic cluster is involved in metal ion binding. Studies with cells expressing various SRCR domain mutants showed that all of the arginines of the basic cluster are involved in ligand binding, suggesting a cooperative binding mechanism. Ligand binding is also dependent on the acidic cluster and Ca2+ ions whose depletion appears to affect ligand binding at least by modulating the electrostatic potential or relative domain orientation. We propose that the SRCR domain dimerization can contribute to the recognition of large ligands by providing a means for the MARCO receptor oligomerization.

About this Structure

2OY3 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition., Ojala JR, Pikkarainen T, Tuuttila A, Sandalova T, Tryggvason K, J Biol Chem. 2007 Jun 1;282(22):16654-66. Epub 2007 Apr 3. PMID:17405873

Page seeded by OCA on Thu Mar 20 18:06:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools