1lsg: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==THREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION SEGMENT OF THE FIBRINOGEN GAMMA CHAIN OBTAINED BY CARRIER PROTEIN-DRIVEN CRYSTALLIZATION== | ==THREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION SEGMENT OF THE FIBRINOGEN GAMMA CHAIN OBTAINED BY CARRIER PROTEIN-DRIVEN CRYSTALLIZATION== | ||
<StructureSection load='1lsg' size='340' side='right' caption='[[1lsg]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1lsg' size='340' side='right'caption='[[1lsg]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lsg]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1lsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsg OCA], [https://pdbe.org/1lsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsg RCSB], [https://www.ebi.ac.uk/pdbsum/1lsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 14: | Line 14: | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/1lsg_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/1lsg_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 28: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1lsg" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1lsg" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Anderson WF]] | ||
[[Category: | [[Category: Patel H]] | ||
Latest revision as of 03:13, 21 November 2024
THREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION SEGMENT OF THE FIBRINOGEN GAMMA CHAIN OBTAINED BY CARRIER PROTEIN-DRIVEN CRYSTALLIZATIONTHREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION SEGMENT OF THE FIBRINOGEN GAMMA CHAIN OBTAINED BY CARRIER PROTEIN-DRIVEN CRYSTALLIZATION
Structural highlights
FunctionLYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have developed a method for crystallizing small functional protein segments so that their three-dimensional structure can be determined by x-ray diffraction analysis. This method consists of linking a small protein segment of unknown tertiary structure to either the amino or carboxyl terminus of a larger carrier protein of known tertiary structure. Crystallization of the small segment is then driven by crystallization of the carrier protein. Using this approach, we have obtained crystals of the human fibrinogen gamma-chain carboxyl-terminal segment linked to the carboxyl terminus of chicken egg white lysozyme. The three-dimensional structure of the carboxyl-terminal segment of the fibrinogen gamma chain was determined by x-ray diffraction analysis at a resolution of 2.4 A. This segment encompasses the recognition site for the integrin alpha IIb beta 3 receptor on activated platelets and for the clumping receptor on pathogenic staphylococci and also bears donor and acceptor sites for factor XIIIa-catalyzed crosslinking of fibrin. Therefore, the structural information derived from our analysis will provide a rational basis for the design of inhibitors of these important functions of fibrinogen. Moreover, carrier protein-driven crystallization will facilitate the determination of the three-dimensional structure of functional segments of other proteins that are, like fibrinogen, difficult to crystallize in toto. Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen gamma chain obtained by carrier protein-driven crystallization.,Donahue JP, Patel H, Anderson WF, Hawiger J Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):12178-82. PMID:7527555[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||