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==THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA==
==THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA==
<StructureSection load='1c5a' size='340' side='right'caption='[[1c5a]], [[NMR_Ensembles_of_Models | 41 NMR models]]' scene=''>
<StructureSection load='1c5a' size='340' side='right'caption='[[1c5a]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_domestica Sus domestica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C5A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c5a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa_domesticus Sus scrofa domesticus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C5A FirstGlance]. <br>
</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=1c5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5a OCA], [https://pdbe.org/1c5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c5a RCSB], [https://www.ebi.ac.uk/pdbsum/1c5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c5a ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1c5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5a OCA], [https://pdbe.org/1c5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c5a RCSB], [https://www.ebi.ac.uk/pdbsum/1c5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CO5_PIG CO5_PIG]] Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C5a also stimulates the locomotion of polymorphonuclear leukocytes (chemokinesis) and direct their migration toward sites of inflammation (chemotaxis).  
[https://www.uniprot.org/uniprot/CO5_PIG CO5_PIG] Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. C5a also stimulates the locomotion of polymorphonuclear leukocytes (chemokinesis) and direct their migration toward sites of inflammation (chemotaxis).
== 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=1c5a 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=1c5a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two-dimensional nuclear magnetic resonance spectra of porcine C5adesArg (73 residues) have been used to construct a list of 34 hydrogen bonds, 27 dihedral angle constraints, and 151 distance constraints, derived from nuclear Overhauser effect data. These constraints were used in restrained molecular dynamics calculations on residues 1-65 of C5a, starting from a folded structure modeled on the crystal structure of a homologous protein, C3a. Forty-one structures have been calculated, which fall into three similar families with few violations of the imposed constraints. Structures in the most populated family have a root-mean-square deviation from the average structure of 1.02 A for the C alpha atoms, with good definition of the internal residues. There is good agreement between the calculated structures and other nuclear magnetic resonance data. The structure is very similar to that recently reported for human C5a [Zuiderweg et al. (1989) Biochemistry 28, 172-185]. Some biological implications of these structures are discussed.
Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data.,Williamson MP, Madison VS Biochemistry. 1990 Mar 27;29(12):2895-905. PMID:2337573<ref>PMID:2337573</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1c5a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus domestica]]
[[Category: Sus scrofa domesticus]]
[[Category: Madison, V S]]
[[Category: Madison VS]]
[[Category: Williamson, M P]]
[[Category: Williamson MP]]
[[Category: Complement factor]]
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