This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lmk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:25, 10 April 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lmk.gif|left|200px]]
 
-
{{Structure
+
==THE STRUCTURE OF A BIVALENT DIABODY==
-
|PDB= 1lmk |SIZE=350|CAPTION= <scene name='initialview01'>1lmk</scene>, resolution 2.6&Aring;
+
<StructureSection load='1lmk' size='340' side='right'caption='[[1lmk]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1lmk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMK 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= L5MK16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmk OCA], [https://pdbe.org/1lmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmk RCSB], [https://www.ebi.ac.uk/pdbsum/1lmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmk ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Evolutionary Conservation ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmk OCA], [http://www.ebi.ac.uk/pdbsum/1lmk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lmk RCSB]</span>
+
[[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/lm/1lmk_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=1lmk ConSurf].
 +
<div style="clear:both"></div>
-
'''THE STRUCTURE OF A BIVALENT DIABODY'''
+
==See Also==
-
 
+
*[[Antibody 3D structures|Antibody 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
BACKGROUND: Diabodies are dimeric antibody fragments. In each polypeptide, a heavy-chain variable domain (VH) is linked to a light-chain variable domain (VL) but unlike single-chain Fv fragments, each antigen-binding site is formed by pairing of one VH and one VL domain from the two different polypeptides. Diabodies thus have two antigen-binding sites, and can be bispecific. Direct structural evidence is lacking for the connections and dimeric interactions between the two polypeptides of the diabody. RESULTS: The 2.6 A resolution structure has been determined for a bivalent diabody with a flexible five-residue polypeptide linker between the (amino-terminal) VH and (carboxy-terminal) VL domains. The asymmetric unit of the crystal consists of four polypeptides comprising two diabodies; for one of these polypeptides the linker can be traced between the VH and VL domains. Within each diabody the two associated VH and VL domains make back-to-back interactions through the VH domains, and there is an extensive VL-VL interface between the two diabodies in the asymmetric unit. CONCLUSIONS: The structure of the diabody is very similar to that which had been predicted by molecular modelling. Diabodies directed against cell-surface antigens should be capable of bringing together two cells, such as in cell-targeted therapy, because the two antigen-binding sites of the diabody are at opposite ends of the molecule and separated by approximately 65 A.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1LMK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMK OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure of a diabody, a bivalent antibody fragment., Perisic O, Webb PA, Holliger P, Winter G, Williams RL, Structure. 1994 Dec 15;2(12):1217-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7704531 7704531]
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Protein complex]]
+
[[Category: Williams RL]]
-
[[Category: Williams, R L.]]
+
-
[[Category: immunoglobulin]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:38 2008''
+

Current revision

THE STRUCTURE OF A BIVALENT DIABODY

PDB ID 1lmk

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/1lmk"
Personal tools