1i8f: Difference between revisions

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[[Image:1i8f.~~jpg~~|left|200px]]

[[Image:1i8f.png|left|200px]]

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~~'''~~THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE~~'''~~

===THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE===

~~==Overview==~~

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~~Sm proteins form the core of small nuclear ribonucleoprotein particles (snRNPs)~~, ~~making them key components of several mRNA-processing assemblies~~, ~~including~~ the ~~spliceosome. We report~~ the 1.~~75-A crystal structure of SmAP, an Sm-like archaeal protein that forms a heptameric ring perforated by a cationic pore~~. ~~In addition to providing direct evidence for such an assembly in eukaryotic snRNPs, this structure (i~~) ~~shows that SmAP homodimers are structurally similar to human Sm heterodimers~~, ~~(ii) supports a gene duplication model of Sm protein evolution, and (iii) offers a model of SmAP bound to single~~-~~stranded RNA (ssRNA) that explains Sm binding~~-~~site specificity. The pronounced electrostatic asymmetry of the SmAP surface imparts directionality to putative SmAP-RNA interactions.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11331747}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11331747 is the PubMed ID number.

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==About this Structure==

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[[Category: Sawaya, M R.]]

[[Category: Beta barrel-like smap monomers form 35-stranded beta-sheet in the heptamer]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:42:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:34:40 2008''

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-[[Image:1i8f.jpg|left|200px]]
+{{Seed}}
+[[Image:1i8f.png|left|200px]]
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 {{STRUCTURE_1i8f|  PDB=1i8f  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE'''
+===THE CRYSTAL STRUCTURE OF A HEPTAMERIC ARCHAEAL SM PROTEIN: IMPLICATIONS FOR THE EUKARYOTIC SNRNP CORE===
-==Overview==
+<!--
-Sm proteins form the core of small nuclear ribonucleoprotein particles (snRNPs), making them key components of several mRNA-processing assemblies, including the spliceosome. We report the 1.75-A crystal structure of SmAP, an Sm-like archaeal protein that forms a heptameric ring perforated by a cationic pore. In addition to providing direct evidence for such an assembly in eukaryotic snRNPs, this structure (i) shows that SmAP homodimers are structurally similar to human Sm heterodimers, (ii) supports a gene duplication model of Sm protein evolution, and (iii) offers a model of SmAP bound to single-stranded RNA (ssRNA) that explains Sm binding-site specificity. The pronounced electrostatic asymmetry of the SmAP surface imparts directionality to putative SmAP-RNA interactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_11331747}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11331747 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11331747}}
 ==About this Structure==
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 [[Category: Sawaya, M R.]]
 [[Category: Beta barrel-like smap monomers form 35-stranded beta-sheet in the heptamer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:42:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:34:40 2008''