1cmi | pdb_00001cmi

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

spinqualitylabelsall models 1cmi, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cmi is a 4 chain structure with sequence from Human. 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. Activity: Nitric-oxide synthase (NADPH dependent), with EC number 1.14.13.39 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. Binds and inhibits the catalytic activity of neuronal nitric oxide synthase. Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. 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. 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 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. 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:10426949 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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