1aud: Difference between revisions

Revision as of 17:36, 30 June 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:1aud.png

Template:STRUCTURE 1aud

U1A-UTRRNA, NMR, 31 STRUCTURESU1A-UTRRNA, NMR, 31 STRUCTURES

Template:ABSTRACT PUBMED 9312034

About this StructureAbout this Structure

1AUD is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1num. Full experimental information is available from OCA.

ReferenceReference

Structural basis of the RNA-binding specificity of human U1A protein., Allain FH, Howe PW, Neuhaus D, Varani G, EMBO J. 1997 Sep 15;16(18):5764-72. PMID:9312034

Page seeded by OCA on Mon Jun 30 17:36:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1aud|  PDB=1aud  |  SCENE=  }}
-'''U1A-UTRRNA, NMR, 31 STRUCTURES'''
+===U1A-UTRRNA, NMR, 31 STRUCTURES===
-==Overview==
+<!--
-The RNP domain is a very common eukaryotic protein domain involved in recognition of a wide range of RNA structures and sequences. Two structures of human U1A in complex with distinct RNA substrates have revealed important aspects of RNP-RNA recognition, but have also raised intriguing questions concerning the origin of binding specificity. The beta-sheet of the domain provides an extensive RNA-binding platform for packing aromatic RNA bases and hydrophobic protein side chains. However, many interactions between functional groups on the single-stranded nucleotides and residues on the beta-sheet surface are potentially common to RNP proteins with diverse specificity and therefore make only limited contribution to molecular discrimination. The refined structure of the U1A complex with the RNA polyadenylation inhibition element reported here clarifies the role of the RNP domain principal specificity determinants (the variable loops) in molecular recognition. The most variable region of RNP proteins, loop 3, plays a crucial role in defining the global geometry of the intermolecular interface. Electrostatic interactions with the RNA phosphodiester backbone involve protein side chains that are unique to U1A and are likely to be important for discrimination. This analysis provides a novel picture of RNA-protein recognition, much closer to our current understanding of protein-protein recognition than that of DNA-protein recognition.
+The line below this paragraph, {{ABSTRACT_PUBMED_9312034}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9312034 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9312034}}
 ==About this Structure==
-AUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1num 1num]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUD OCA].
+AUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1num 1num]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUD OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Rnp domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:42:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:36:36 2008''