1bql

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

1bql is a 3 chain structure with sequence from Colinus virginianus and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S. Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment. Proteins. 1996 Sep;26(1):55-65. PMID:8880929 doi:<55::AID-PROT5>3.0.CO;2-F 10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Colinus virginianus | Large Structures | Mus musculus | Chacko S | Davies DR

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF AN ANTI-HEL FAB FRAGMENT COMPLEXED WITH BOBWHITE QUAIL LYSOZYME==
-<StructureSection load='1bql' size='340' side='right' caption='[[1bql]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='1bql' size='340' side='right'caption='[[1bql]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bql]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Colvi Colvi] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BQL FirstGlance]. <br>
+<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>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1bql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bql RCSB], [http://www.ebi.ac.uk/pdbsum/1bql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bql ProSAT]</span></td></tr>
+<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>
+<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>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 14: / Line 15: @@
   <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/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 32: @@
 ==See Also==
 *[[Lysozyme 3D structures|Lysozyme 3D structures]]
-*[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Colvi]]
+[[Category: Colinus virginianus]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Chacko, S]]
+[[Category: Mus musculus]]
-[[Category: Davies, D R]]
+[[Category: Chacko S]]
-[[Category: Anti-lysozyme]]
+[[Category: Davies DR]]
-[[Category: Antibody-antigen complex]]
-[[Category: Bobwhite quail]]
-[[Category: Hyhel-5]]

1bql

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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