1bc0: Difference between revisions

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<StructureSection load='1bc0' size='340' side='right'caption='[[1bc0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1bc0' size='340' side='right'caption='[[1bc0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BC0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1bc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc0 OCA], [https://pdbe.org/1bc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc0 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=1bc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bc0 OCA], [https://pdbe.org/1bc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bc0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ANXA5_RAT ANXA5_RAT]] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.  
[https://www.uniprot.org/uniprot/ANXA5_RAT ANXA5_RAT] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
== 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=1bc0 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=1bc0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Annexin V belongs to a family of eukaryotic calcium-dependent membrane-binding proteins. The calcium-binding sites at the annexin-membrane interface have been investigated in some detail; however, little is known about the functional roles of highly conserved interfacial residues that do not coordinate calcium themselves. In the present study, the importance of tryptophan 185, and threonine or serine at positions 72, 144, 228, and 303, in rat annexin V is investigated by site-directed mutagenesis, X-ray crystallography, and functional assays. The high-resolution crystal structures of the mutants show that the mutations do not cause structural perturbations of the annexin molecule itself or disappearance of bound calcium ions from calcium-binding sites. The assays indicate that relative to wild-type annexin V, loss of the methyl substituent at position 72 (Thr72--&gt;Ser) has no effect while loss of the hydroxyl group (Thr72--&gt;Ala or Thr72--&gt;Lys) causes reduction of membrane binding. Multiple lysine substitutions (e.g., Thr72,Ser144,Ser228,Ser303--&gt;Lys) have a greater adverse effect than the single lysine mutation, suggesting that in annexin V the introduction of potentially favorable electrostatic interactions between the lysine side chains and the net negatively charged membrane surface is not sufficient to overcome the loss of the hydroxyl side chains. Replacement of the unique tryptophan, Trp185, by alanine similarly decreases membrane binding affinity. Taken together, the data suggest that the side chains mutated in this study contribute to phospholipid binding and participate directly in intermolecular contacts with phospholipid membrane components.
Mutational and crystallographic analyses of interfacial residues in annexin V suggest direct interactions with phospholipid membrane components.,Campos B, Mo YD, Mealy TR, Li CW, Swairjo MA, Balch C, Head JF, Retzinger G, Dedman JR, Seaton BA Biochemistry. 1998 Jun 2;37(22):8004-10. PMID:9609693<ref>PMID:9609693</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bc0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Annexin 3D structures|Annexin 3D structures]]
*[[Annexin 3D structures|Annexin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Head, J F]]
[[Category: Rattus norvegicus]]
[[Category: Li, C W]]
[[Category: Head JF]]
[[Category: Mo, Y D]]
[[Category: Li CW]]
[[Category: Seaton, B A]]
[[Category: Mo YD]]
[[Category: Swairjo, M A]]
[[Category: Seaton BA]]
[[Category: Calcium binding protein]]
[[Category: Swairjo MA]]
[[Category: Calcium-binding protein]]
[[Category: Phospholipid membrane binding protein]]

Latest revision as of 09:34, 7 February 2024

RECOMBINANT RAT ANNEXIN V, W185A MUTANTRECOMBINANT RAT ANNEXIN V, W185A MUTANT

Structural highlights

1bc0 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANXA5_RAT This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1bc0, resolution 2.00Å

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