1ha1: Difference between revisions

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 <StructureSection load='1ha1' size='340' side='right'caption='[[1ha1]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ha1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HA1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ha1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HA1 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ha1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ha1 OCA], [https://pdbe.org/1ha1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ha1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ha1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ha1 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ha1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ha1 OCA], [https://pdbe.org/1ha1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ha1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ha1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ha1 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN]] Amyotrophic lateral sclerosis;Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>   The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>
+[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Amyotrophic lateral sclerosis;Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>   The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN]] Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.<ref>PMID:17229681</ref>
+[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.<ref>PMID:17229681</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ha1 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Heterogeneous ribonucleoprotein A1 (hnRNP A1) is an abundant eukaryotic nuclear RNA binding protein. A1 is involved in the packaging of pre-mRNA into hnRNP particles, transport of poly A+ mRNA from the nucleus to the cytoplasm and may modulate splice site selection. The crystal structure of A1(RBD1,2) reveals two independently-folded RNA binding domains (RBDs) connected by a flexible linker. Both RBDs are structurally homologous to the U1A(RBD1), and have their RNA binding platforms oriented in an anti-parallel fashion. The anti-parallel arrangement of the A1 RNA binding platforms suggests mechanisms for RNA condensation and ways of bringing together distant RNA sequences for RNA metabolism such as splicing or transport.
-Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 A resolution.,Shamoo Y, Krueger U, Rice LM, Williams KR, Steitz TA Nat Struct Biol. 1997 Mar;4(3):215-22. PMID:9164463<ref>PMID:9164463</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ha1" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Krueger, U]]
+[[Category: Krueger U]]
-[[Category: Rice, L]]
+[[Category: Rice L]]
-[[Category: Shamoo, Y]]
+[[Category: Shamoo Y]]
-[[Category: Steitz, T A]]
+[[Category: Steitz TA]]
-[[Category: Williams, K R]]
+[[Category: Williams KR]]
-[[Category: Hnrnp]]
-[[Category: Nuclear protein]]
-[[Category: Rbd]]
-[[Category: Ribonucleoprotein]]
-[[Category: Rna binding]]
-[[Category: Rnp]]
-[[Category: Rrm]]