1dfj: Difference between revisions
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==RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A== | ==RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A== | ||
<StructureSection load='1dfj' size='340' side='right' caption='[[1dfj]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1dfj' size='340' side='right'caption='[[1dfj]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dfj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. The September 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ribonuclease A'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_9 10.2210/rcsb_pdb/mom_2008_9]. The November 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Toll-like Receptors'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_11 10.2210/rcsb_pdb/mom_2011_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DFJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dfj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. The September 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ribonuclease A'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_9 10.2210/rcsb_pdb/mom_2008_9]. The November 2011 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Toll-like Receptors'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2011_11 10.2210/rcsb_pdb/mom_2011_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DFJ FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[RNase A|RNase A]] | *[[RNase A|RNase A]] | ||
*[[Ribonuclease|Ribonuclease]] | |||
*[[Ribonuclease inhibitor|Ribonuclease inhibitor]] | |||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 09:58, 10 October 2019
RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE ARIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A
Structural highlights
Function[RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] [RINI_PIG] Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe leucine-rich repeat is a recently characterized structural motif used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing. We present here the crystal structure at 2.5 A resolution of the complex between ribonuclease A and ribonuclease inhibitor, a protein built entirely of leucine-rich repeats. The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel beta-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs. The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands. A structural basis of the interactions between leucine-rich repeats and protein ligands.,Kobe B, Deisenhofer J Nature. 1995 Mar 9;374(6518):183-6. PMID:7877692[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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