| First Author | Jiang W | Year | 1997 |
| Journal | Gene | Volume | 189 |
| Issue | 1 | Pages | 65-71 |
| PubMed ID | 9161413 | Mgi Jnum | J:40070 |
| Mgi Id | MGI:87409 | Doi | 10.1016/s0378-1119(96)00834-7 |
| Citation | Jiang W, et al. (1997) Correlation of the exon/intron organization to the secondary structures of the protease domain of mouse meprin alpha subunit. Gene 189(1):65-71 |
| abstractText | Metalloendopeptidases of the astacin family contain a homologous protease domain of about 200 amino acids. We now report the genomic structure corresponding to the protease domain for one member of this family, the mouse meprin alpha subunit. This is the first such description for the mammalian meprin subunits. It consists of four small exons (76 to 222 base pairs) and three large introns (2.9 to 4.2 kilobases). The exon/intron organization correlates well with the secondary structure elements of the domain as predicted by computer modeling. Exon Ep1 contains beta strand I, and Ep2 consists of helix A and beta strands II-III. Ep3 corresponds to beta strands IV-V and helix B. Ep4 correlates with helices C and D. Introns Ip1 and Ip2 are present at the beginning of helix A and beta strand IV, respectively, and Ip3 is between helices B and C. Similar analyses of sequences previously published by others, have extended this correlation to other astacin family members from different organisms. The relationship between gene and protein structures within the astacin family provide novel information on the evolution of this family in relation to other gene families. |
