1cmi: Difference between revisions

Latest revision as of 07:24, 14 February 2024

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

Structural highlights

1cmi is a 4 chain structure with sequence from Homo sapiens and Rattus norvegicus. This structure supersedes the now removed PDB entry 1b1w. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.^[5] ^[6] ^[7] ^[8] Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.^[9] ^[10] ^[11] ^[12] 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.^[13] ^[14] ^[15] ^[16]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022
↑ Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417
↑ Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200
↑ Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022
↑ Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417
↑ Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200
↑ Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022
↑ Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417
↑ Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200
↑ Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631
↑ Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022
↑ Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417
↑ Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631

[2] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022

[3] Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417

[4] Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200

[5] Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631

[6] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022

[7] Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417

[8] Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200

[9] Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631

[10] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022

[11] Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417

[12] Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200

[13] Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 1999 Mar;3(3):287-96. PMID:10198631

[14] Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R. Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell. 2004 Jun;5(6):575-85. PMID:15193260 doi:10.1016/j.ccr.2004.05.022

[15] Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R. Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. PMID:15891768 doi:10.1038/sj.embor.7400417

[16] Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200

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@@ Line 1: / Line 1: @@
-[[Image:1cmi.gif|left|200px]]<br />
-<applet load="1cmi" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1cmi, resolution 2.5&Aring;" />
-'''STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE'''<br />
-==Overview==
+==STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE==
-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.
+<StructureSection load='1cmi' size='340' side='right'caption='[[1cmi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
-==Disease==
+<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>
-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]], HDL cholesterol level QTL 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606613 606613]], Lung cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604050 604050]]
+</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>
+<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>
-==About this Structure==
+</table>
-CMI 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 superseeds the now removed PDB entry 1B1W. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMI OCA].
+== Function ==
+[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>
-==Reference==
+== Evolutionary Conservation ==
-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]
+[[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/cm/1cmi_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=1cmi ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Clardy, J.]]
+[[Category: Rattus norvegicus]]
-[[Category: Guo, W.]]
+[[Category: Clardy J]]
-[[Category: Jaffery, S.]]
+[[Category: Guo W]]
-[[Category: Liang, J.]]
+[[Category: Jaffery S]]
-[[Category: Snyder, S.]]
+[[Category: Liang J]]
-[[Category: dynein light chain]]
+[[Category: Snyder S]]
-[[Category: lc8]]
-[[Category: nnos]]
-[[Category: pin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:23:21 2007''

1cmi: Difference between revisions

Latest revision as of 07:24, 14 February 2024

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

Structural highlights

Function

Evolutionary Conservation

References

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