Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs Export

@article{citeulike:4960596, abstract = {The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B′, D 1 , D 2 , D 3 , E, F, and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs (snRNAs). These proteins share a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Crystal structures of two Sm protein complexes, D 3 B and D 1 D 2 , show that these proteins have a common fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β sheet, and the D 1 D 2 and D 3 B dimers superpose closely in their core regions, including the dimer interfaces. The crystal structures suggest that the seven Sm proteins could form a closed ring and the snRNAs may be bound in the positively charged central hole.}, author = {Kambach, C. and Walke, S. and Young, R. and Avis, J. and Delafortelle, E. and Raker, V. and Luhrmann, R. and Li, J. and Nagai, K.}, citeulike-article-id = {4960596}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0092-8674(00)80550-4}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092867400805504}, day = {05}, doi = {10.1016/S0092-8674(00)80550-4}, issn = {00928674}, journal = {Cell}, keywords = {crystal, protein, sm, snrnps, spliceosome}, month = {February}, number = {3}, pages = {375--387}, posted-at = {2009-06-25 21:33:08}, priority = {2}, title = {Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs}, url = {http://dx.doi.org/10.1016/S0092-8674(00)80550-4}, volume = {96}, year = {1999} }

TY - JOUR ID - citeulike:4960596 L3 - citeulike-article-id:4960596 N2 - The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B′, D 1 , D 2 , D 3 , E, F, and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs (snRNAs). These proteins share a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Crystal structures of two Sm protein complexes, D 3 B and D 1 D 2 , show that these proteins have a common fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β sheet, and the D 1 D 2 and D 3 B dimers superpose closely in their core regions, including the dimer interfaces. The crystal structures suggest that the seven Sm proteins could form a closed ring and the snRNAs may be bound in the positively charged central hole. IS - 3 JF - Cell SN - 00928674 EP - 387 TI - Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs VL - 96 SP - 375 KW - crystal KW - protein KW - sm KW - snrnps KW - spliceosome AU - Kambach, C AU - Walke, S AU - Young, R AU - Avis, J AU - Delafortelle, E AU - Raker, V AU - Luhrmann, R AU - Li, J AU - Nagai, K PY - 1999/02/05/ UR - http://dx.doi.org/10.1016/S0092-8674(00)80550-4 ER -