3bav: Difference between revisions

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-{{Seed}}
-[[Image:3bav.png|left|200px]]
-<!--
+==Crystal structure of L26A/D28N mutant of Human acidic fibroblast growth factor==
-The line below this paragraph, containing "STRUCTURE_3bav", creates the "Structure Box" on the page.
+<StructureSection load='3bav' size='340' side='right'caption='[[3bav]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3bav]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BAV FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_3bav|  PDB=3bav  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bav OCA], [https://pdbe.org/3bav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bav RCSB], [https://www.ebi.ac.uk/pdbsum/3bav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bav ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FGF1_HUMAN FGF1_HUMAN] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.<ref>PMID:8663044</ref> <ref>PMID:16597617</ref> <ref>PMID:20145243</ref>
+== 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/3bav_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3bav ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Turn secondary structure is essential to the formation of globular protein architecture. Turn structures are, however, much more complex than either alpha-helix or beta-sheet, and the thermodynamics and folding kinetics are poorly understood. Type I beta-turns are the most common type of reverse turn, and they exhibit a statistical consensus sequence of Asx-Pro-Asx-Gly (where Asx is Asp or Asn). A comprehensive series of individual and combined Asx mutations has been constructed within three separate type I 3:5 G1 bulge beta-turns in human fibroblast growth factor-1, and their effects on structure, stability, and folding have been determined. The results show a fundamental logical OR relationship between the Asx residues in the motif, involving H-bond interactions with main-chain amides within the turn. These interactions can be modulated by additional interactions with residues adjacent to the turn at positions i+4 and i+6. The results show that the Asx residues in the turn motif make a substantial contribution to the overall stability of the protein, and the Asx logical OR relationship defines a redundant system that can compensate for deleterious point mutations. The results also show that the stability of the turn is unlikely to be the prime determinant of formation of turn structure in the folding transition state.
-===Crystal structure of L26A/D28N mutant of Human acidic fibroblast growth factor===
+A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif.,Lee J, Dubey VK, Longo LM, Blaber M J Mol Biol. 2008 Apr 4;377(4):1251-64. Epub 2008 Jan 31. PMID:18308335<ref>PMID:18308335</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3bav" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18308335}}, adds the Publication Abstract to the page
+*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18308335 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18308335}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BAV is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BAV OCA].
-==Reference==
-<ref group="xtra">PMID:18308335</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Blaber, M.]]
+[[Category: Large Structures]]
-[[Category: Lee, J.]]
+[[Category: Blaber M]]
-[[Category: Acetylation]]
+[[Category: Lee J]]
-[[Category: Angiogenesis]]
-[[Category: Beta-trefoil]]
-[[Category: Developmental protein]]
-[[Category: Differentiation]]
-[[Category: Growth factor]]
-[[Category: Heparin-binding]]
-[[Category: Hormone]]
-[[Category: Mitogen]]
-[[Category: Polymorphism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:19:23 2009''