View source for 2baf


==Bovine Fibrinogen alpha-C Domain==
<StructureSection load='2baf' size='340' side='right'caption='[[2baf]]' scene=''>
== Structural highlights ==
<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>
</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=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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ba/2baf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=2baf ConSurf].
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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Fibrinogen|Fibrinogen]]
== References ==
<references/>
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Burton RA]]