1rjh: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rjh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1rjh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJH FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1rjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjh OCA], [https://pdbe.org/1rjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjh RCSB], [https://www.ebi.ac.uk/pdbsum/1rjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjh 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=1rjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjh OCA], [https://pdbe.org/1rjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjh RCSB], [https://www.ebi.ac.uk/pdbsum/1rjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/1rjh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/1rjh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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=1rjh 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=1rjh ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tetranectin is a homotrimeric protein containing a C-type lectin-like domain. This domain (TN3) can bind calcium, but in the absence of calcium, the domain binds a number of kringle-type protein ligands. Two of the calcium-coordinating residues are also critical for binding plasminogen kringle 4 (K4). The structure of the calcium free-form of TN3 (apoTN3) has been determined by NMR. Compared to the structure of the calcium-bound form of TN3 (holoTN3), the core region of secondary structural elements is conserved, while large displacements occur in the loops involved in calcium or K4 binding. A conserved proline, which was found to be in the cis conformation in holoTN3, is in apoTN3 predominantly in the trans conformation. Backbone dynamics indicate that, in apoTN3 especially, two of the three calcium-binding loops and two of the three K4-binding residues exhibit increased flexibility, whereas no such flexibility is observed in holoTN3. In the 20 best nuclear magnetic resonance structures of apoTN3, the residues critical for K4 binding span a large conformational space. Together with the relaxation data, this indicates that the K4-ligand-binding site in apoTN3 is not preformed. | |||
Structure of the plasminogen kringle 4 binding calcium-free form of the C-type lectin-like domain of tetranectin.,Nielbo S, Thomsen JK, Graversen JH, Jensen PH, Etzerodt M, Poulsen FM, Thogersen HC Biochemistry. 2004 Jul 13;43(27):8636-43. PMID:15236571<ref>PMID:15236571</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1rjh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 07:51, 17 October 2024
Structure of the Calcium Free Form of the C-type Lectin-like Domain of TetranectinStructure of the Calcium Free Form of the C-type Lectin-like Domain of Tetranectin
Structural highlights
FunctionTETN_HUMAN Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTetranectin is a homotrimeric protein containing a C-type lectin-like domain. This domain (TN3) can bind calcium, but in the absence of calcium, the domain binds a number of kringle-type protein ligands. Two of the calcium-coordinating residues are also critical for binding plasminogen kringle 4 (K4). The structure of the calcium free-form of TN3 (apoTN3) has been determined by NMR. Compared to the structure of the calcium-bound form of TN3 (holoTN3), the core region of secondary structural elements is conserved, while large displacements occur in the loops involved in calcium or K4 binding. A conserved proline, which was found to be in the cis conformation in holoTN3, is in apoTN3 predominantly in the trans conformation. Backbone dynamics indicate that, in apoTN3 especially, two of the three calcium-binding loops and two of the three K4-binding residues exhibit increased flexibility, whereas no such flexibility is observed in holoTN3. In the 20 best nuclear magnetic resonance structures of apoTN3, the residues critical for K4 binding span a large conformational space. Together with the relaxation data, this indicates that the K4-ligand-binding site in apoTN3 is not preformed. Structure of the plasminogen kringle 4 binding calcium-free form of the C-type lectin-like domain of tetranectin.,Nielbo S, Thomsen JK, Graversen JH, Jensen PH, Etzerodt M, Poulsen FM, Thogersen HC Biochemistry. 2004 Jul 13;43(27):8636-43. PMID:15236571[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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