Structural highlights
Function
[DNAL1_CHLRE] Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.[1]
Publication Abstract from PubMed
Dynein motors are biologically important bio-nanomachines, and many atomic resolution structures of cytoplasmic dynein components from different organisms have been analyzed by X-ray crystallography, cryo-EM, and NMR spectroscopy. This review provides a historical perspective of structural studies of cytoplasmic and axonemal dynein including accessory proteins. We describe representative structural studies of every component of dynein and summarize them as a structural atlas that classifies the cytoplasmic and axonemal dyneins. Based on our review of all dynein structures in the Protein Data Bank, we raise two important points for understanding the two types of dynein motor and discuss the potential prospects of future structural studies.
Structural atlas of dynein motors at atomic resolution.,Toda A, Tanaka H, Kurisu G Biophys Rev. 2018 Feb 24. pii: 10.1007/s12551-018-0402-y. doi:, 10.1007/s12551-018-0402-y. PMID:29478092[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Benashski SE, Patel-King RS, King SM. Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the gamma heavy chain. Biochemistry. 1999 Jun 1;38(22):7253-64. PMID:10353837 doi:http://dx.doi.org/10.1021/bi990466y
- ↑ Toda A, Tanaka H, Kurisu G. Structural atlas of dynein motors at atomic resolution. Biophys Rev. 2018 Feb 24. pii: 10.1007/s12551-018-0402-y. doi:, 10.1007/s12551-018-0402-y. PMID:29478092 doi:http://dx.doi.org/10.1007/s12551-018-0402-y
