1nnt: Difference between revisions
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<StructureSection load='1nnt' size='340' side='right'caption='[[1nnt]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1nnt' size='340' side='right'caption='[[1nnt]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nnt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1nnt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NNT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1nnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nnt OCA], [https://pdbe.org/1nnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nnt RCSB], [https://www.ebi.ac.uk/pdbsum/1nnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nnt ProSAT]</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=1nnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nnt OCA], [https://pdbe.org/1nnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nnt RCSB], [https://www.ebi.ac.uk/pdbsum/1nnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nnt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TRFE_CHICK TRFE_CHICK] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=1nnt ConSurf]. | </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=1nnt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Transferrin 3D structures|Transferrin 3D structures]] | *[[Transferrin 3D structures|Transferrin 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dewan | [[Category: Dewan JC]] | ||
[[Category: Mikami | [[Category: Mikami B]] | ||
[[Category: Sacchettini | [[Category: Sacchettini JC]] | ||
Revision as of 11:51, 10 April 2024
STRUCTURAL EVIDENCE FOR A PH-SENSITIVE DI-LYSINE TRIGGER IN THE HEN OVOTRANSFERRIN N-LOBE: IMPLICATIONS FOR TRANSFERRIN IRON RELEASESTRUCTURAL EVIDENCE FOR A PH-SENSITIVE DI-LYSINE TRIGGER IN THE HEN OVOTRANSFERRIN N-LOBE: IMPLICATIONS FOR TRANSFERRIN IRON RELEASE
Structural highlights
FunctionTRFE_CHICK Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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