2hnp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:33, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2hnp.jpg|left|200px]]
 
-
{{Structure
+
==CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B==
-
|PDB= 2hnp |SIZE=350|CAPTION= <scene name='initialview01'>2hnp</scene>, resolution 2.85&Aring;
+
<StructureSection load='2hnp' size='340' side='right'caption='[[2hnp]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2hnp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HNP FirstGlance]. <br>
-
|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]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hnp OCA], [https://pdbe.org/2hnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hnp RCSB], [https://www.ebi.ac.uk/pdbsum/2hnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hnp ProSAT]</span></td></tr>
-
}}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/2hnp_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hnp ConSurf].
 +
<div style="clear:both"></div>
-
'''CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B'''
+
==See Also==
-
 
+
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.
+
__TOC__
-
 
+
</StructureSection>
-
==Disease==
+
-
Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176885 176885]], Insulin resistance, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176885 176885]]
+
-
 
+
-
==About this Structure==
+
-
2HNP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNP OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure of human protein tyrosine phosphatase 1B., Barford D, Flint AJ, Tonks NK, Science. 1994 Mar 11;263(5152):1397-404. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8128219 8128219]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Protein-tyrosine-phosphatase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Barford D]]
-
[[Category: Barford, D.]]
+
[[Category: Flint AJ]]
-
[[Category: Flint, A J.]]
+
[[Category: Tonks NK]]
-
[[Category: Tonks, N K.]]
+
-
[[Category: hydrolase(phosphorylation)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:12 2008''
+

Current revision

CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B

PDB ID 2hnp

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/2hnp"
Personal tools