1b8k

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(New page: 200px<br /> <applet load="1b8k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8k, resolution 2.15&Aring;" /> '''NEUROTROPHIN-3 FROM...)
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[[Image:1b8k.gif|left|200px]]<br />
 
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<applet load="1b8k" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b8k, resolution 2.15&Aring;" />
 
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'''NEUROTROPHIN-3 FROM HUMAN'''<br />
 
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==Overview==
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==Neurotrophin-3 from Human==
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The development and sustenance of specific neuronal populations in the, peripheral and central nervous systems are controlled through the binding, of neurotrophic factors to high-affinity cell surface receptors. The, neurotrophins (nerve growth factor, NGF; brain-derived neurotrophic, factor, BDNF; neurotrophin 3, NT3; and neurotrophin 4, NT4) are dimeric, molecules which share approximately 50% sequence identity. The crystal, structure of the murine NGF homodimer [McDonald et al. (1991) Nature 354, 411-414] indicated that the dimer interface corresponds to regions of high, sequence conservation throughout the neurotrophin family. This potential, compatibility was duly exploited for the production in vitro of, noncovalent heterodimers between the different neurotrophins, [Radziejewski, C., &amp; Robinson, R.C. (1993) Biochemistry 32, 13350-13356;, Jungbluth et al. (1994) Eur. J. Biochem. 221, 677-685]. Here, we report, the X-ray structure at 2.3 A resolution of one such heterodimer, between, human BDNF, and human NT3. The NGF, BDNF, and NT3 protomers share the same, topology and are structurally equivalent in regions which contribute to, the dimer interface in line with the propensity of the neurotrophins to, form heterodimers. Analysis of the structure of regions of the BDNF/NT3, heterodimer involved in receptor specificity led us to conclude that, heterodimer binding to p75 involves distant binding sites separately, located on each protomer of the heterodimer. In contrast, heterodimer, interactions with the trk receptors probably utilize hybrid binding sites, comprised of residues contributed by both protomers in the heterodimer., The existence of such hybrid binding sites for the trk receptor provides, an explanation for the lower activity of the BDNF/NT3 heterodimer in, comparison to the homodimers.(ABSTRACT TRUNCATED AT 250 WORDS)
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<StructureSection load='1b8k' size='340' side='right'caption='[[1b8k]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b8k]] 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=1B8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B8K FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8k OCA], [https://pdbe.org/1b8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b8k RCSB], [https://www.ebi.ac.uk/pdbsum/1b8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b8k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NTF3_HUMAN NTF3_HUMAN] Seems to promote the survival of visceral and proprioceptive sensory neurons.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/1b8k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1b8k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The neurotrophins are growth factors that are involved in the development and survival of neurons. Neurotrophin release by a target tissue results in neuron growth along the neurotrophin concentration gradient, culminating in the eventual innervation of the target tissue. These activities are mediated through trk cell surface receptors. We have determined the structures of the heterodimer formed between brain-derived neurotrophic factor (BDNF) and neurotrophin 4 (NT4), as well as the structure of homodimer of NT4. We also present the structure of the Neurotrophin 3 homodimer, which is refined to higher resolution than previously published. These structures provide the first views of the architecture of the NT4 protomer. Comparison of the surface of a model of the BDNF homodimer with the structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors. In particular, there exists an analogous region on the surface of each neurotrophin that is likely to be involved in trk receptor binding. Variations in sequence on the periphery of this common region serve to confer trk receptor specificity.
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==About this Structure==
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The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site.,Robinson RC, Radziejewski C, Spraggon G, Greenwald J, Kostura MR, Burtnick LD, Stuart DI, Choe S, Jones EY Protein Sci. 1999 Dec;8(12):2589-97. PMID:10631974<ref>PMID:10631974</ref>
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1B8K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B8K OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer., Robinson RC, Radziejewski C, Stuart DI, Jones EY, Biochemistry. 1995 Apr 4;34(13):4139-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7703225 7703225]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1b8k" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Choe, S.]]
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[[Category: Jones, E.Y.]]
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[[Category: Radziejewski, C.]]
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[[Category: Robinson, R.C.]]
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[[Category: Stuart, D.I.]]
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[[Category: complex (growth factor/growth factor)]]
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[[Category: neurotrophin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:07:11 2007''
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==See Also==
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*[[Neurotrophin|Neurotrophin]]
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*[[Neutrotrophin|Neutrotrophin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Choe S]]
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[[Category: Jones EY]]
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[[Category: Radziejewski C]]
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[[Category: Robinson RC]]
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[[Category: Stuart DI]]

Current revision

Neurotrophin-3 from Human

PDB ID 1b8k

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