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3q0p

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Revision as of 14:59, 24 December 2014

Crystal structure of the PUMILIO-homology domain from Human PUMILIO1 in complex with hunchback NRE

Structural highlights

3q0p is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3q0l, 3q0m, 3q0n, 3q0o, 3q0q, 3q0r, 3q0s
Gene:	PUM1, KIAA0099, PUMH1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PUM1_HUMAN] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity).

Publication Abstract from PubMed

Human PUMILIO1 (PUM1) and PUMILIO2 (PUM2) are members of the PUMILIO/FBF (PUF) family that regulate specific target mRNAs posttranscriptionally. Recent studies have identified mRNA targets associated with human PUM1 and PUM2. Here, we explore the structural basis of natural target RNA recognition by human PUF proteins through crystal structures of the RNA-binding domains of PUM1 and PUM2 in complex with four cognate RNA sequences, including sequences from p38alpha and erk2 MAP kinase mRNAs. We observe three distinct modes of RNA binding around the fifth RNA base, two of which are different from the prototypical 1 repeat:1 RNA base binding mode previously identified with model RNA sequences. RNA-binding affinities of PUM1 and PUM2 are not affected dramatically by the different binding modes in vitro. However, these modes of binding create structurally variable recognition surfaces that suggest a mechanism in vivo for recruitment of downstream effector proteins defined by the PUF:RNA complex.

Alternate modes of cognate RNA recognition by human PUMILIO proteins.,Lu G, Hall TM Structure. 2011 Mar 9;19(3):361-7. PMID:21397187^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lu G, Hall TM. Alternate modes of cognate RNA recognition by human PUMILIO proteins. Structure. 2011 Mar 9;19(3):361-7. PMID:21397187 doi:10.1016/j.str.2010.12.019

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3q0p"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q0p RCSB], [http://www.ebi.ac.uk/pdbsum/3q0p PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PUM1_HUMAN PUM1_HUMAN]] Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3q0p

From Proteopedia

Revision as of 14:59, 24 December 2014

Crystal structure of the PUMILIO-homology domain from Human PUMILIO1 in complex with hunchback NRE

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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