Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

• HOME
• SETUP
• FAQ
• ABOUT
• GLOSSARY
• WHAT'S NEW
• FEEDBACK

Dynein_light Dynein light chain type 1

SMART accession number:	SM01375
Description:	-
Interpro abstract (IPR001372):	Dynein is a multisubunit microtubule-dependent motor enzyme that acts as the force generating protein of eukaryotic cilia and flagella. The cytoplasmic isoform of dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein is composed of a number of ATP-binding large subunits (see IPR004273 ), intermediate size subunits and small subunits. Among the small subunits, there is a family of highly conserved proteins which make up this family [ (PUBMED:7744782) (PUBMED:8628263) ]. Both type 1 (DLC1) and 2 (DLC2) dynein light chains have a similar two-layer alpha-beta core structure consisting of beta-alpha(2)-beta-X-beta(2) [ (PUBMED:10426949) (PUBMED:14561217) ].
GO process:	microtubule-based process (GO:0007017)
GO component:	dynein complex (GO:0030286)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 4882 Dynein_light domains in 4751 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Dynein_light domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Dynein_light domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Dynein_light domain in the selected taxonomic class.

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Tochio H, Ohki S, Zhang Q, Li M, Zhang M
  • Solution structure of a protein inhibitor of neuronal nitric oxide synthase.
  • Nat Struct Biol. 1998; 5: 965-9
  • Display abstract

  • The structure of the neuronal nitric oxide synthase inhibitory protein, PIN(protein inhibitor of nNOS), has been determined by NMR spectroscopy. TwoN-terminal antiparallel alpha-helices pack against a four-stranded antiparallelbeta-sheet in the C-terminal region of the protein, forming a two-layeralpha/beta plait. The three dimensional structure of PIN resembles the fold ofthe B-chain of aspartylglucosaminidase. A non-prolyl cis peptide bond was foundbetween Pro 52 and Thr 53 of the protein. PIN has a large solvent-exposedhydrophobic surface that contains a cavity and is rimmed with positive charges.This surface may serve as the primary target-binding region for thismulti-functional regulatory protein.

• Structure (3D structures containing this domain)

• 3D Structures of Dynein_light domains in PDB

  PDB code	Main view	Title
  1cmi		STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE
  1f3c		REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)
  1f95		SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
  1f96		SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
  1pwj		Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
  1pwk		Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
  1re6		Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands
  1rhw		The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila
  1yo3		1.65 Angstrom Structure of the Dynein Light Chain 1 from Plasmodium falciparum
  2p2t		Crystal structure of dynein light chain LC8 bound to residues 123-138 of intermediate chain IC74
  2pg1		Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex
  2xqq		Human dynein light chain (DYNLL2) in complex with an in vitro evolved peptide (Ac-SRGTQTE).
  3bri		Crystal Structure of apo-LC8
  3brl		Crystal Structure of LC8 S88E / Swa
  3dvh		LC8 Point mutant K36P
  3dvp		Pak1 peptide bound LC8
  3dvt		Biochemical and structural characterization of the PAK1- LC8 interaction
  3e2b		Crystal structure of Dynein Light chain LC8 in complex with a peptide derived from Swallow
  3fm7		Quaternary Structure of Drosophila melanogaster IC/Tctex-1/LC8; Allosteric Interactions of Dynein Light Chains with Dynein Intermediate Chain
  3glw		Quaternary Structure of Drosophila melanogaster IC/Tctex-1/LC8; Allosteric Interactions of Dynein Light Chains with Dynein Intermediate Chain
  3p8m		Human dynein light chain (DYNLL2) in complex with an in vitro evolved peptide dimerized by leucine zipper
  3rjs		Crystal structure of Dynein Light Chain 8a (DLC8) from Toxoplasma gondii at 1.5 A resolution
  3zke		Structure of LC8 in complex with Nek9 peptide
  3zkf		Structure of LC8 in complex with Nek9 phosphopeptide
  4d07		4D07
  4ds1		The Structure of a Yeast Dyn2-Nup159 Complex and the Molecular Basis for the Dynein Light Chain - Nuclear Pore Interaction
  4ht6		The Structure of a Yeast Dynein Dyn2-Pac11 Complex and Effect on Single Molecule Dynein Motor Activity
  4qh7		4QH7
  4qh8		4QH8
  5e0l		5E0L
  5e0m		5E0M
  5fwz		5FWZ
  5fx0		5FX0

• Links (links to other resources describing this domain)

• INTERPRO	IPR001372
  PFAM	Dynein_light

Send comments to Ivica Letunic