Protein Family Models

This entry represents a TIG-like domain found in the suppressor of hairless protein. [1]. 15297877. Crystal structure of the nuclear effector of Notch signaling,. CSL, bound to DNA.. Kovall RA, Hendrickson WA;. EMBO J. 2004;23:3441-3451.. [2]. 16530044. Structural basis for cooperativity in recruitment of MAML. coactivators to Notch transcription complexes.. Nam Y, Sliz P, Song L, Aster JC, Blacklow SC;. Cell. 2006;124:973-983.. [3]. 18381292. RAM-induced allostery facilitates assembly of a notch pathway. active transcription complex.. Friedmann DR, Wilson JJ, Kovall RA;. J Biol Chem. 2008;283:14781-14791.. [4]. 19866488. Thermodynamic and structural insights into CSL-DNA complexes.. Friedmann DR, Kovall RA;. Protein Sci. 2010;19:34-46.. [5]. 20972443. Structural and mechanistic insights into cooperative assembly of. dimeric Notch transcription complexes.. Arnett KL, Hass M, McArthur DG, Ilagan MX, Aster JC, Kopan R,. Blacklow SC;. Nat Struct Mol Biol. 2010;17:1312-1317. (from Pfam)

Date:

2024-08-14

Phyto-Amp is a family of phytopathogenic wall-less bacterial antigenic membrane proteins [1]. The bacteria are limited to the phloem and pose a major threat to agriculture worldwide. They are transmitted in a persistent, propagative manner by phloem-sucking Hemipteran insects. Phytoplasma membrane proteins are in direct contact with hosts and are assumed to be involved in determining vector specificity. Phyto-Amp is thought to be one family of proteins that mediates such specificity. The proteins appear to be encoded by circular extrachromosomal elements, at least one of which is a plasmid [2]. [1]. 11782508. Immunodominant membrane proteins from two phytoplasmas in the. aster yellows clade (chlorante aster yellows and clover. phyllody) are highly divergent in the major hydrophilic region.. Barbara DJ, Morton A, Clark MF, Davies DL;. Microbiology. 2002;148:157-167.. [2]. 21799902. The major antigenic membrane protein of "Candidatus Phytoplasma. asteris" selectively interacts with ATP synthase and actin of. leafhopper vectors.. Galetto L, Bosco D, Balestrini R, Genre A, Fletcher J, Marzachi. C;. PLoS One. 2011;6:e22571. (from Pfam)

Date:

2024-08-14

The MamL-1 domain is a polypeptide of up to 70 residues, numbers 15-67 of which adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors. [1,2]. [1]. 16530044. Structural basis for cooperativity in recruitment of MAML. coactivators to Notch transcription complexes.. Nam Y, Sliz P, Song L, Aster JC, Blacklow SC;. Cell. 2006;124:973-983.. [2]. 22325781. Conformational locking upon cooperative assembly of notch. transcription complexes.. Choi SH, Wales TE, Nam Y, O'Donovan DJ, Sliz P, Engen JR,. Blacklow SC;. Structure. 2012;20:340-349. (from Pfam)

Date:

2024-08-14

This family represents Asterix proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes [1]. The PAT complex acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins [1]. Asterix is the substrate-interacting subunit of the PAT complex and associates with the first TMD of the nascent chain. The PAT complex favors the binding to TMDs with exposed hydrophilic amino acids within the lipid bilayer and provides a membrane-embedded partially hydrophilic environment in which TMD1 binds [1]. [1]. 32814900. An intramembrane chaperone complex facilitates membrane protein. biogenesis.. Chitwood PJ, Hegde RS;. Nature. 2020;584:630-634. (from Pfam)

Date:

2024-08-14

The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR [1] and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase [2]. [1]. 12795601. Nuclear magnetic resonance structure of a prototype Lin12-Notch. repeat module from human Notch1.. Vardar D, North CL, Sanchez-Irizarry C, Aster JC, Blacklow SC;. Biochemistry. 2003;42:7061-7067.. [2]. 15262980. The Lin12-notch repeats of pregnancy-associated plasma protein-A. bind calcium and determine its proteolytic specificity.. Boldt HB, Kjaer-Sorensen K, Overgaard MT, Weyer K, Poulsen CB,. Sottrup-Jensen L, Conover CA, Giudice LC, Oxvig C;. J Biol Chem. 2004;279:38525-38531. (from Pfam)

Date:

2024-08-14

GRAM and VASt domain-containing protein such as mammalian Aster proteins (or GRAM domain-containing proteins), which act as cholesterol transporters that mediate non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER)

Date:

2024-09-03