1bql

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:26, 30 October 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bql.gif|left|200px]]
 
-
{{Structure
+
==STRUCTURE OF AN ANTI-HEL FAB FRAGMENT COMPLEXED WITH BOBWHITE QUAIL LYSOZYME==
-
|PDB= 1bql |SIZE=350|CAPTION= <scene name='initialview01'>1bql</scene>, resolution 2.6&Aring;
+
<StructureSection load='1bql' size='340' side='right'caption='[[1bql]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
+
<table><tr><td colspan='2'>[[1bql]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Colinus_virginianus Colinus virginianus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQL FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bql OCA], [https://pdbe.org/1bql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bql RCSB], [https://www.ebi.ac.uk/pdbsum/1bql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bql ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bql OCA], [http://www.ebi.ac.uk/pdbsum/1bql PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bql RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/LYSC_COLVI LYSC_COLVI] 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.
 +
== 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/bq/1bql_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=1bql ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The HyHEL-5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg-white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL-5, an antihen egg-white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side-chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL-5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side-chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL-5 is similar to that in previously determined lysozyme-HyHEL-5 complexes.
-
'''STRUCTURE OF AN ANTI-HEL FAB FRAGMENT COMPLEXED WITH BOBWHITE QUAIL LYSOZYME'''
+
Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment.,Chacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S Proteins. 1996 Sep;26(1):55-65. PMID:8880929<ref>PMID:8880929</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1bql" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The HyHEL-5 antibody has more than a thousandfold lower affinity for bobwhite quail lysozyme (BWQL) than for hen egg-white lysozyme (HEL). Four sequence differences exist between BWQL and HEL, of which only one is involved in the interface with the Fab. The structure of bobwhite quail lysozyme has been determined in the uncomplexed state in two different crystal forms and in the complexed state with HyHEL-5, an antihen egg-white lysozyme Fab. Similar backbone conformations are observed in the three molecules of the two crystal forms of uncomplexed BWQL, although they show considerable variability in side-chain conformation. A relatively mobile segment in uncomplexed BWQL is observed to be part of the HyHEL-5 epitope. No major backbone conformational differences are observed in the lysozyme upon complex formation, but side-chain conformational differences are seen in surface residues that are involved in the interface with the antibody. The hydrogen bonding in the interface between BWQL and HyHEL-5 is similar to that in previously determined lysozyme-HyHEL-5 complexes.
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-
==About this Structure==
+
== References ==
-
1BQL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Colinus_virginianus Colinus virginianus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQL OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment., Chacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S, Proteins. 1996 Sep;26(1):55-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8880929 8880929]
+
[[Category: Colinus virginianus]]
[[Category: Colinus virginianus]]
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Protein complex]]
+
[[Category: Chacko S]]
-
[[Category: Chacko, S.]]
+
[[Category: Davies DR]]
-
[[Category: Davies, D R.]]
+
-
[[Category: complex (antibody/antigen)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:06:14 2008''
+

Current revision

STRUCTURE OF AN ANTI-HEL FAB FRAGMENT COMPLEXED WITH BOBWHITE QUAIL LYSOZYME

PDB ID 1bql

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bql"
Personal tools