1nt3: Difference between revisions

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-[[Image:1nt3.png|left|200px]]
-<!--
+==HUMAN NEUROTROPHIN-3==
-The line below this paragraph, containing "STRUCTURE_1nt3", creates the "Structure Box" on the page.
+<StructureSection load='1nt3' size='340' side='right'caption='[[1nt3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1nt3]] 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=1NT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NT3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nt3 OCA], [https://pdbe.org/1nt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nt3 RCSB], [https://www.ebi.ac.uk/pdbsum/1nt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nt3 ProSAT]</span></td></tr>
-{{STRUCTURE_1nt3|  PDB=1nt3  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NTF3_HUMAN NTF3_HUMAN] Seems to promote the survival of visceral and proprioceptive sensory neurons.
+== 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/nt/1nt3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nt3 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Neurotrophin-3 (NT-3) is a cystine knot growth factor that promotes the survival, proliferation, and differentiation of developing neurons and is a potential therapeutic for neurodegenerative diseases. To clarify the structural basis of receptor specificity and the role of neurotrophin dimerization in receptor activation, the structure of the NT-3 homodimer was determined using X-ray crystallography. The orthorhombic crystals diffract to 2.4 A, with dimer symmetry occurring about a crystallographic 2-fold axis. The overall structure of NT-3 resembles that of the other neurotrophins, NGF and BDNF; each protomer forms a twisted four-stranded beta sheet, with three intertwined disulfide bonds. There are notable differences, however, between NT-3 and NGF in the surface loops and in three functionally important regions, shown in previous mutagenesis studies to be critical for binding. One such difference implies that NT-3's binding affinity and specificity depend on a novel hydrogen bond between Gln 83, a residue important for binding specificity with TrkC, and Arg 103, a residue crucial for binding affinity with TrkC. NT-3's extensive dimer interface buries much of the otherwise solvent-accessible hydrophobic surface area and suggests that the dimeric state is stabilized through the formation of this hydrophobic core. A comparison of the dimer interface between the NT-3 homodimer and the BDNF/NT-3 heterodimer reveals similar patterns of hydrogen bonds and nonpolar contacts, which reinforces the notion that the evolutionarily conserved neurotrophin interface resulted from the need for receptor dimerization in signal initiation.
-===HUMAN NEUROTROPHIN-3===
+Crystal structure of neurotrophin-3 homodimer shows distinct regions are used to bind its receptors.,Butte MJ, Hwang PK, Mobley WC, Fletterick RJ Biochemistry. 1998 Dec 1;37(48):16846-52. PMID:9836577<ref>PMID:9836577</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1nt3" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9836577}}, adds the Publication Abstract to the page
+*[[Neurotrophin|Neurotrophin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9836577 is the PubMed ID number.
+*[[Neutrotrophin|Neutrotrophin]]
--->
+== References ==
-{{ABSTRACT_PUBMED_9836577}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-[[1nt3]] is a 1 chain structure with 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=1NT3 OCA].
-==Reference==
-<ref group="xtra">PMID:009836577</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Butte, M J.]]
+[[Category: Large Structures]]
-[[Category: Fletterick, R J.]]
+[[Category: Butte MJ]]
-[[Category: Hwang, P K.]]
+[[Category: Fletterick RJ]]
-[[Category: Mobley, W C.]]
+[[Category: Hwang PK]]
-[[Category: Cystine knot]]
+[[Category: Mobley WC]]
-[[Category: Growth factor]]
-[[Category: Hormone-growth factor-neuropeptide complex]]
-[[Category: Neurotrophin]]