Sema domain

Sema domain, immunoglobulin domain (Ig), short basic domain
Identifiers
Symbol Sema
Pfam PF01403
InterPro IPR001627
PROSITE PDOC51004
SCOP 1olz
SUPERFAMILY 1olz

The Sema domain is a structural domain of semaphorins, which are a large family of secreted and transmembrane proteins, some of which function as repellent signals during axon guidance. Sema domains also occur in the hepatocyte growth factor receptor (Uniprot: P08581), Plexin-A3 [1] (Uniprot: P51805) and in viral proteins.

CD100 (also called SEMA4D) is associated with PTPase and serine kinase activity. CD100 increases PMA, CD3 and CD2 induced T cell proliferation, increases CD45 induced T cell adhesion, induces B cell homotypic adhesion and down-regulates B cell expression of CD23.

The Sema domain is characterised by a conserved set of cysteine residues, which form four disulfide bonds to stabilise the structure. The Sema domain fold is a variation of the beta propeller topology, with seven blades radially arranged around a central axis. Each blade contains a four- stranded (strands A to D) antiparallel beta sheet. The inner strand of each blade (A) lines the channel at the centre of the propeller, with strands B and C of the same repeat radiating outward, and strand D of the next repeat forming the outer edge of the blade. The large size of the Sema domain is not due to a single inserted domain but results from the presence of additional secondary structure elements inserted in most of the blades. The Sema domain uses a 'loop and hook' system to close the circle between the first and the last blades. The blades are constructed sequentially with an N-terminal beta- strand closing the circle by providing the outermost strand (D) of the seventh (C-terminal) blade. The beta-propeller is further stabilized by an extension of the N-terminus, providing an additional, fifth beta-strand on the outer edge of blade 6.[2][3][4]

CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/).

Human proteins containing this domain

MET; MST1R; PLXNA1; PLXNA2; PLXNA3; PLXNA4; PLXNB1; PLXNB2; PLXNB3; PLXND1; SEMA3A; SEMA3B; SEMA3C; SEMA3D; SEMA3E; SEMA3F; SEMA3G; SEMA4A; SEMA4B; SEMA4C; SEMA4D; SEMA4F; SEMA4G; SEMA5A; SEMA5B; SEMA6A; SEMA6B; SEMA6C; SEMA6D; SEMA7A;

References

  1. ↑ Goodman CS; Winberg ML; Noordermeer JN; Tamagnone L; Comoglio PM; Spriggs MK; Tessier-Lavigne M (1998). "Plexin A is a neuronal semaphorin receptor that controls axon guidance". Cell. 95 (7): 903–916. doi:10.1016/S0092-8674(00)81715-8. PMID 9875845.
  2. ↑ Nikolov DB; Himanen JP; Rajashankar KR; Lu M; Antipenko A; Lesniak J; Barton WA; Hoemme C; Puschel AW; van Leyen K; Nardi-Dei V (2003). "Structure of the semaphorin-3A receptor binding module". Neuron. 39 (4): 589–598. doi:10.1016/S0896-6273(03)00502-6. PMID 12925274.
  3. ↑ Stuart DI; Jones EY; Harlos K; Esnouf RM; Davis SJ; Love CA; Mavaddat N (2003). "The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D". Nat. Struct. Biol. 10 (10): 843–848. doi:10.1038/nsb977. PMID 12958590.
  4. ↑ Lazarus RA; Kirchhofer D; Stamos J; Yao X; Wiesmann C (2004). "Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor". EMBO J. 23 (12): 2325–2335. doi:10.1038/sj.emboj.7600243. PMC 423285Freely accessible. PMID 15167892.

This article incorporates text from the public domain Pfam and InterPro IPR001627

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