Summary for 1CMI
| Entry DOI | 10.2210/pdb1cmi/pdb |
| Descriptor | Dynein light chain 1, cytoplasmic, Nitric oxide synthase 1 (3 entities in total) |
| Functional Keywords | pin, lc8, nnos, dynein light chain, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 22737.97 |
| Authors | Liang, J.,Guo, W.,Jaffery, S.,Snyder, S.,Clardy, J. (deposition date: 1999-05-06, release date: 2000-02-21, Last modification date: 2024-02-14) |
| Primary citation | Liang, J.,Jaffrey, S.R.,Guo, W.,Snyder, S.H.,Clardy, J. Structure of the PIN/LC8 dimer with a bound peptide. Nat.Struct.Biol., 6:735-740, 1999 Cited by PubMed Abstract: 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. PubMed: 10426949DOI: 10.1038/11501 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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