Protein Family Models

This entry contains a series of TPR repeats. [1]. 11709169. Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization. Steegborn C, Danot O, Huber R, Clausen T;. Structure. 2001;9:1051-1060. [2]. 22171003. Inscuteable and NuMA proteins bind competitively to Leu-Gly-Asn repeat-enriched protein (LGN) during asymmetric cell divisions. Culurgioni S, Alfieri A, Pendolino V, Laddomada F, Mapelli M;. Proc Natl Acad Sci U S A. 2011;108:20998-21003. [3]. 22215984. Structural basis of response regulator inhibition by a bacterial anti-activator protein. Baker MD, Neiditch MB;. PLoS Biol. 2011;9:e1001226. [4]. 23526880. Structural basis of Rap phosphatase inhibition by Phr peptides. Gallego del Sol F, Marina A;. PLoS Biol. 2013;11:e1001511. [5]. 23519214. Structural basis for kinesin-1:cargo recognition. Pernigo S, Lamprecht A, Steiner RA, Dodding MP;. Science. 2013;340:356-359. [6]. 23526881. Conformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptors. Parashar V, Jeffrey PD, Neiditch MB;. PLoS Biol. 2013;11:e1001512. (from Pfam)

Date:

2024-10-16

The soluble NSF attachment protein (SNAP) proteins are involved in vesicular transport between the endoplasmic reticulum and Golgi apparatus [1]. They act as adaptors between SNARE (integral membrane SNAP receptor) proteins and NSF (N-ethylmaleimide-sensitive factor) [2]. They are structurally similar to TPR repeats [2]. [1]. 8455721. SNAP family of NSF attachment proteins includes a brain-specific isoform. Whiteheart SW, Griff IC, Brunner M, Clary DO, Mayer T, Buhrow SA, Rothman JE;. Nature. 1993;362:353-355. [2]. 10445030. Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly. Rice LM, Brunger AT;. Mol Cell. 1999;4:85-95. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14