2k11: Difference between revisions

Revision as of 04:07, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2k11.png

Template:STRUCTURE 2k11

Solution structure of human pancreatic ribonucleaseSolution structure of human pancreatic ribonuclease

Template:ABSTRACT PUBMED 18495155

About this StructureAbout this Structure

2K11 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition., Kover KE, Bruix M, Santoro J, Batta G, Laurents DV, Rico M, J Mol Biol. 2008 Jun 20;379(5):953-65. Epub 2008 Apr 25. PMID:18495155

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OCA

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 {{STRUCTURE_2k11|  PDB=2k11  |  SCENE=  }}
-'''Solution structure of human pancreatic ribonuclease'''
+===Solution structure of human pancreatic ribonuclease===
-==Overview==
+<!--
-Human pancreatic ribonuclease (RNase 1) is expressed in many tissues; has several important enzymatic and biological activities, including efficient cleavage of single-stranded RNA, double-stranded RNA and double-stranded RNA-DNA hybrids, digestion of dietary RNA, regulation of vascular homeostasis, inactivation of the HIV, activation of immature dendritic cells and induction of cytokine production; and furthermore shows potential as an anti-tumor agent. The solution structure and dynamics of uncomplexed, wild-type RNase 1 have been determined by NMR spectroscopy methods to better understand these activities. The family of 20 structures determined on the basis of 6115 unambiguous nuclear Overhauser enhancements is well resolved (pairwise backbone RMSD=1.07 A) and has the classic RNase A type of tertiary structure. Important structural differences compared with previously determined crystal structures of RNase 1 variants or inhibitor-bound complexes are observed in the conformation of loop regions and side chains implicated in the enzymatic as well as biological activities and binding to the cytoplasmic RNase inhibitor. Multiple side chain conformations observed for key surface residues are proposed to be crucial for membrane binding as well as translocation and efficient RNA hydrolysis. (15)N-(1)H relaxation measurements interpreted with the standard and our extended Lipari-Szabo formalism reveal rigid regions and identify more dynamic loop regions. Some of the most dynamic areas are key for binding to the cytoplasmic RNase inhibitor. This finding and the important differences observed between the structure in solution and that bound to the inhibitor are indications that RNase 1 to inhibitor binding can be better described by the "induced fit" model rather than the rigid "lock-into-key" mechanism. Translational diffusion measurements reveal that RNase 1 is predominantly dimeric above 1 mM concentration; the possible implications of this dimeric state for the remarkable biological properties of RNase 1 are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_18495155}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18495155 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18495155}}
 ==About this Structure==
-K11 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K11 OCA].
+K11 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K11 OCA].
 ==Reference==
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 [[Category: Nuclease]]
 [[Category: Secreted]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 09:50:50 2008''
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