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3e2b

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Revision as of 08:13, 9 February 2022

Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow

Structural highlights

3e2b is a 2 chain structure with sequence from Drome. This structure supersedes the now removed PDB entry 2p1k. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2p1k
Gene:	ctp, Cdlc1, ddlc1, CG6998 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DYL1_DROME] Acts as a non-catalytic accessory component of a dynein complex (By similarity). [SWA_DROME] Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.^[1]

Evolutionary Conservation

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

Publication Abstract from PubMed

Dynein light chain LC8 is a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein and myosin molecular motors but appears to have a broader role in multiple protein complexes unrelated to molecular motors. LC8 binds to two families of targets: those having a KXTQT sequence fingerprint and those having a GIQVD fingerprint. All known LC8 binding partners containing these fingerprints share a common binding site on LC8 that raises the question of what determines binding specificity. Here, we present the crystal structure of apo-LC8 at 1.7-A resolution, which, when compared with the crystal structures of several LC8 complexes, gives insight into the mechanism underlying the binding diversity of LC8. Peptide binding is associated with a shift in quaternary structure that expands the hydrophobic binding surface available to the ligand, in addition to changes in tertiary structure and ordering of LC8 around the binding groove. The observed quaternary shift suggests a mechanism by which binding at one of the two identical sites can influence binding at the other. NMR spectra of titrations with peptides from each fingerprint family show evidence of allosteric interaction between the two binding sites, to a differing degree in the two ligand families. Allosteric interaction between the binding sites may be a mechanism to promote simultaneous binding of ligands from the same family, providing a physiological role for the two fingerprints.

The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8.,Benison G, Karplus PA, Barbar E J Mol Biol. 2008 Dec 26;384(4):954-66. Epub 2008 Oct 11. PMID:18948118^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chao YC, Donahue KM, Pokrywka NJ, Stephenson EC. Sequence of swallow, a gene required for the localization of bicoid message in Drosophila eggs. Dev Genet. 1991;12(5):333-41. PMID:1806330 doi:http://dx.doi.org/10.1002/dvg.1020120502
↑ Benison G, Karplus PA, Barbar E. The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J Mol Biol. 2008 Dec 26;384(4):954-66. Epub 2008 Oct 11. PMID:18948118 doi:10.1016/j.jmb.2008.09.083

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3e2b"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow==
-<StructureSection load='3e2b' size='340' side='right' caption='[[3e2b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3e2b' size='340' side='right'caption='[[3e2b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3e2b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p1k 2p1k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E2B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3e2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p1k 2p1k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p1k|2p1k]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p1k|2p1k]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctp, Cdlc1, ddlc1, CG6998 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctp, Cdlc1, ddlc1, CG6998 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2b OCA], [http://pdbe.org/3e2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e2b RCSB], [http://www.ebi.ac.uk/pdbsum/3e2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2b ProSAT]</span></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=3e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2b OCA], [https://pdbe.org/3e2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2b RCSB], [https://www.ebi.ac.uk/pdbsum/3e2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME]] Acts as a non-catalytic accessory component of a dynein complex (By similarity). [[http://www.uniprot.org/uniprot/SWA_DROME SWA_DROME]] Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.<ref>PMID:1806330</ref>
+[[https://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME]] Acts as a non-catalytic accessory component of a dynein complex (By similarity). [[https://www.uniprot.org/uniprot/SWA_DROME SWA_DROME]] Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.<ref>PMID:1806330</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Dynein|Dynein]]
+*[[Dynein 3D structures|Dynein 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Drome]]
+[[Category: Large Structures]]
 [[Category: Barbar, E]]
 [[Category: Benison, G]]

3e2b

From Proteopedia

Revision as of 08:13, 9 February 2022

Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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