2yvi: Difference between revisions

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 ==Crystal structure of a death domain of human ankryn protein==
-<StructureSection load='2yvi' size='340' side='right' caption='[[2yvi]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
+<StructureSection load='2yvi' size='340' side='right'caption='[[2yvi]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yvi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YVI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yvi]] 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=2YVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YVI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANK1, ANK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANK1, ANK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<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=2yvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvi OCA], [http://pdbe.org/2yvi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yvi RCSB], [http://www.ebi.ac.uk/pdbsum/2yvi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yvi ProSAT], [http://www.topsan.org/Proteins/RSGI/2yvi TOPSAN]</span></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=2yvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvi OCA], [https://pdbe.org/2yvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yvi RCSB], [https://www.ebi.ac.uk/pdbsum/2yvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yvi ProSAT], [https://www.topsan.org/Proteins/RSGI/2yvi TOPSAN]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:[http://omim.org/entry/182900 182900]]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.<ref>PMID:8640229</ref> <ref>PMID:11102985</ref>
+[[https://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:[https://omim.org/entry/182900 182900]]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive.<ref>PMID:8640229</ref> <ref>PMID:11102985</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.<ref>PMID:12456646</ref>   Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.<ref>PMID:12456646</ref>
+[[https://www.uniprot.org/uniprot/ANK1_HUMAN ANK1_HUMAN]] Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.<ref>PMID:12456646</ref>   Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.<ref>PMID:12456646</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 24: / Line 24: @@
 ==See Also==
-*[[Ankyrin|Ankyrin]]
+*[[Ankyrin 3D structures|Ankyrin 3D structures]]
 == References ==
 <references/>
@@ Line 30: / Line 30: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Bessho, Y]]
 [[Category: Chen, L]]