2baf

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[[Image:2baf.png|left|200px]]
 
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==Bovine Fibrinogen alpha-C Domain==
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The line below this paragraph, containing "STRUCTURE_2baf", creates the "Structure Box" on the page.
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<StructureSection load='2baf' size='340' side='right'caption='[[2baf]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2baf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BAF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2baf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2baf OCA], [https://pdbe.org/2baf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2baf RCSB], [https://www.ebi.ac.uk/pdbsum/2baf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2baf ProSAT]</span></td></tr>
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{{STRUCTURE_2baf| PDB=2baf | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FIBA_BOVIN FIBA_BOVIN] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/2baf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2baf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The NMR solution structure of the bovine fibrinogen alphaC-domain fragment, including residues Aalpha374-538, reveals a type-I' beta-hairpin, restricted at the base by a C423-C453 disulfide linkage and a short turn preceding C423. Although both faces of the hairpin are formed mainly by hydrophilic residues, one of them is uncharged while the other has a characteristic pattern of charged residues which are highly conserved among vertebrate species. Chemical shift indexing and relaxation data indicate the presence of a collapsed hydrophobic region next to the hairpin that includes approximately 30 residues with slower concerted motion and higher content of nonpolar residues and, according to a previous study (Tsurupa, G., Tsonev, L., and Medved, L. (2002) Biochemistry 41, 6449-6459), may cooperate with the hairpin to form a compact cooperative unit (domain). Structure and relaxation data show that the region between C423 and C453 is populated by both random coil and beta-structure, suggesting that the cooperative structure in the isolated alphaC-domain is intrinsically unstable. This observation is in agreement with a very low energy of stabilization of the Aalpha374-538 fragment determined in unfolding experiments. The low stability of the alphaC-domain suggests a possible explanation for the previously observed intra- and intermolecular interactions of these domains in fibrinogen and fibrin.
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===Bovine Fibrinogen alpha-C Domain===
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Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR.,Burton RA, Tsurupa G, Medved L, Tjandra N Biochemistry. 2006 Feb 21;45(7):2257-66. PMID:16475814<ref>PMID:16475814</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16475814}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2baf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16475814 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16475814}}
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==About this Structure==
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[[2baf]] is a 1 chain structure of [[Fibrinogen]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BAF OCA].
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==See Also==
==See Also==
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*[[Fibrinogen]]
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*[[Fibrinogen|Fibrinogen]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:16475814</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Burton, R A.]]
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[[Category: Large Structures]]
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[[Category: Beta hairpin]]
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[[Category: Burton RA]]
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[[Category: Blood clotting]]
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[[Category: Fibrinogen]]
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Current revision

Bovine Fibrinogen alpha-C Domain

PDB ID 2baf

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