1cmi

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[[Image:1cmi.gif|left|200px]]<br /><applet load="1cmi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cmi, resolution 2.5&Aring;" />
 
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'''STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE'''<br />
 
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==Overview==
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==STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE==
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The structure of the protein known both as neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), and also as the 8 kDa dynein light chain (LC8) has been solved by X-ray diffraction. Two PIN/LC8 monomers related by a two-fold axis form a rectangular dimer. Two pairs of alpha-helices cover opposite faces, and each pair of helices packs against a beta-sheet with five antiparallel beta-strands. Each five-stranded beta-sheet contains four strands from one monomer and a fifth strand from the other monomer. A 13-residue peptide from nNOS is bound to the dimer in a deep hydrophobic groove as a sixth antiparallel beta-strand. The structure provides key insights into dimerization of and peptide binding by the multifunctional PIN/LC8 protein.
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<StructureSection load='1cmi' size='340' side='right'caption='[[1cmi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1cmi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b1w 1b1w]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMI FirstGlance]. <br>
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Known diseases associated with this structure: Colorectal cancer, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604258 604258]], Esophageal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604050 604050]], Lung cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604050 604050]]
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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]] 2.5&#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=1cmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmi OCA], [https://pdbe.org/1cmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmi RCSB], [https://www.ebi.ac.uk/pdbsum/1cmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmi ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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1CMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1B1W. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMI OCA].
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== Function ==
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[https://www.uniprot.org/uniprot/DYL1_HUMAN DYL1_HUMAN] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref>
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==Reference==
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== Evolutionary Conservation ==
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Structure of the PIN/LC8 dimer with a bound peptide., Liang J, Jaffrey SR, Guo W, Snyder SH, Clardy J, Nat Struct Biol. 1999 Aug;6(8):735-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10426949 10426949]
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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/cm/1cmi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1cmi ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Clardy, J.]]
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[[Category: Rattus norvegicus]]
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[[Category: Guo, W.]]
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[[Category: Clardy J]]
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[[Category: Jaffery, S.]]
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[[Category: Guo W]]
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[[Category: Liang, J.]]
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[[Category: Jaffery S]]
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[[Category: Snyder, S.]]
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[[Category: Liang J]]
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[[Category: dynein light chain]]
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[[Category: Snyder S]]
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[[Category: lc8]]
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[[Category: nnos]]
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[[Category: pin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:33 2008''
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Current revision

STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE

PDB ID 1cmi

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