1jln

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jln.gif|left|200px]]<br /><applet load="1jln" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1jln.gif|left|200px]]
-
caption="1jln, resolution 1.81&Aring;" />
+
 
-
'''Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7'''<br />
+
{{Structure
 +
|PDB= 1jln |SIZE=350|CAPTION= <scene name='initialview01'>1jln</scene>, resolution 1.81&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1JLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLN OCA].
+
1JLN 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=1JLN OCA].
==Reference==
==Reference==
-
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation., Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ, J Mol Biol. 2001 Aug 17;311(3):557-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11493009 11493009]
+
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation., Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ, J Mol Biol. 2001 Aug 17;311(3):557-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11493009 11493009]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
Line 24: Line 33:
[[Category: ptpbr7]]
[[Category: ptpbr7]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:03 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:06 2008''

Revision as of 10:05, 20 March 2008


PDB ID 1jln

Drag the structure with the mouse to rotate
, resolution 1.81Å
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7


Overview

Protein tyrosine phosphatases PTP-SL and PTPBR7 are isoforms belonging to cytosolic membrane-associated and to receptor-like PTPs (RPTPs), respectively. They represent a new family of PTPs with a major role in activation and translocation of MAP kinases. Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. This interaction is strictly dependent upon a kinase interaction motif (KIM) (residues 224-239) situated at the N terminus of the PTP-SL catalytic domain. We report the first crystal structure of the catalytic domain for a member of this family (PTP-SL, residues 254-549, identical with residues 361-656 of PTPBR7), providing an example of an RPTP with single cytoplasmic domain, which is monomeric, having an unhindered catalytic site. In addition to the characteristic PTP-core structure, PTP-SL has an N-terminal helix, possibly orienting the KIM motif upon interaction with the target ERK2. An unusual residue in the catalytically important WPD loop promotes formation of a hydrophobically and electrostatically stabilised clamp. This could induce increased rigidity to the WPD loop and therefore reduced catalytic activity, in agreement with our kinetic measurements. A docking model based on the PTP-SL structure suggests that, in the complex with ERK2, the phosphorylation of PTP-SL should be accomplished first. The subsequent dephosphorylation of ERK2 seems to be possible only if a conformational rearrangement of the two interacting partners takes place.

About this Structure

1JLN is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation., Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ, J Mol Biol. 2001 Aug 17;311(3):557-68. PMID:11493009

Page seeded by OCA on Thu Mar 20 12:05:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools