1y8g

From Proteopedia

(Difference between revisions)

Revision as of 06:50, 25 April 2018

Catalytic and ubiqutin-associated domains of MARK2/PAR-1: Inactive double mutant with selenomethionine

Structural highlights

1y8g is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1zmu, 1zmv, 1zmw
Gene:	MARK2 (Buffalo rat)
Activity:	Transferase, with EC number 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Ser/Thr kinase MARK2 phosphorylates tau protein at sites that cause detachment from microtubules in Alzheimer neurofibrillary degeneration. Homologs of MARK2 include Par-1 in C. elegans and Drosophila, which generates embryonic polarity. We report the X-ray structure of the catalytic and ubiquitin-associated domains (UBA) of human MARK2. The activity was altered by mutations in the ATP binding site and/or activation loop. The catalytic domain shows the small and large lobes typical of kinases. The substrate cleft is in an inactive, open conformation in the inactivated and the wild-type structure. The UBA domain is attached via a taut linker to the large lobe of the kinase domain and leans against a hydrophobic patch on the small lobe. The UBA structure is unusual because the orientation of its third helix is inverted, relative to previous structures. Possible implications of the structure for the regulation of kinase activity are discussed.

Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1.,Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E Structure. 2006 Feb;14(2):173-83. PMID:16472737^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E. Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1. Structure. 2006 Feb;14(2):173-83. PMID:16472737 doi:10.1016/j.str.2005.09.022

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y8g"

@@ Line 1: / Line 1: @@
 ==Catalytic and ubiqutin-associated domains of MARK2/PAR-1: Inactive double mutant with selenomethionine==
 <StructureSection load='1y8g' size='340' side='right' caption='[[1y8g]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MARK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8g OCA], [http://pdbe.org/1y8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y8g RCSB], [http://www.ebi.ac.uk/pdbsum/1y8g PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8g OCA], [http://pdbe.org/1y8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y8g RCSB], [http://www.ebi.ac.uk/pdbsum/1y8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y8g ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y8/1y8g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y8/1y8g_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1y8g" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
 == References ==
 <references/>

1y8g

From Proteopedia

Revision as of 06:50, 25 April 2018

Catalytic and ubiqutin-associated domains of MARK2/PAR-1: Inactive double mutant with selenomethionine

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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