Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.[5][6][7][8]
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.[8]
DYNLL1 has been shown to interact with:
PDB gallery
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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
2pg1: Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex
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