8KCQ

Solution structures of the N-terminal divergent caplonin homology (NN-CH) domains of human intraflagellar transport protein 54

Summary for 8KCQ

• Entry DOI: 10.2210/pdb8kcq/pdb
• NMR Information: BMRB: 36589
• Descriptor: TRAF3-interacting protein 1 (1 entity in total)
• Functional Keywords: nn-ch domain, intraflagellar transport (ift) machinery, ift54, ciliopathy, structural genomics, psi-2, protein structure initiative, riken structural genomics/proteomics initiative, rsgi, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 15401.02

Authors

Dang, W.,Kuwasako, K.,He, F.,Takahashi, M.,Tsuda, K.,Nagata, T.,Tanaka, A.,Kobayashi, N.,Kigawa, T.,Guentert, P.,Shirouzu, M.,Yokoyama, S.,Muto, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2023-08-08, release date: 2024-05-22)

Primary citation

Kuwasako, K.,Dang, W.,He, F.,Takahashi, M.,Tsuda, K.,Nagata, T.,Tanaka, A.,Kobayashi, N.,Kigawa, T.,Guntert, P.,Shirouzu, M.,Yokoyama, S.,Muto, Y.
1 H, 13 C, and 15 N resonance assignments and solution structure of the N-terminal divergent calponin homology (NN-CH) domain of human intraflagellar transport protein 54.
Biomol.Nmr Assign., 18:71-78, 2024

PubMed Abstract: The intraflagellar transport (IFT) machinery plays a crucial role in the bidirectional trafficking of components necessary for ciliary signaling, such as the Hedgehog, Wnt/PCR, and cAMP/PKA systems. Defects in some components of the IFT machinery cause dysfunction, leading to a wide range of human diseases and developmental disorders termed ciliopathies, such as nephronophthisis. The IFT machinery comprises three sub-complexes: BBsome, IFT-A, and IFT-B. The IFT protein 54 (IFT54) is an important component of the IFT-B sub-complex. In anterograde movement, IFT54 binds to active kinesin-II, walking along the cilia microtubule axoneme and carrying the dynein-2 complex in an inactive state, which works for retrograde movement. Several mutations in IFT54 are known to cause Senior-Loken syndrome, a ciliopathy. IFT54 possesses a divergent Calponin Homology (CH) domain termed as NN-CH domain at its N-terminus. However, several aspects of the function of the NN-CH domain of IFT54 are still obscure. Here, we report the H, N, and C resonance assignments of the NN-CH domain of human IFT54 and its solution structure. The NN-CH domain of human IFT54 adopts essentially the α1-α2-α3-α4-α5 topology as that of mouse IFT54, whose structure was determined by X-ray crystallographic study. The structural information and assignments obtained in this study shed light on the molecular function of the NN-CH domain in IFT54.

PubMed: 38551798
DOI: 10.1007/s12104-024-10170-w

Experimental method

SOLUTION NMR