1shm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:48, 6 November 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1shm.png|left|200px]]
 
-
<!--
+
==Convergent solutions to VHH domain stabilization from natural and in vitro evolution==
-
The line below this paragraph, containing "STRUCTURE_1shm", creates the "Structure Box" on the page.
+
<StructureSection load='1shm' size='340' side='right'caption='[[1shm]], [[Resolution|resolution]] 1.90&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'>[[1shm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHM 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]] 1.9&#8491;</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=1shm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shm OCA], [https://pdbe.org/1shm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shm RCSB], [https://www.ebi.ac.uk/pdbsum/1shm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shm ProSAT]</span></td></tr>
-
{{STRUCTURE_1shm| PDB=1shm | SCENE= }}
+
</table>
 +
== 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/sh/1shm_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=1shm ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The diversity of natural antibodies is limited by the genetic mechanisms that engender diversity and the functional requirements of antigen binding. Using an in vitro-evolved autonomous heavy chain variable domain (V(H)H-RIG), we have investigated the limits of structurally-tolerated diversity in the three complementarity-determining regions and a fourth loop within the third framework region. We determined the X-ray crystal structure of the V(H)H-RIG domain at 1.9A resolution and used it to guide the design of phage-displayed libraries encompassing the four loops. The libraries were subjected to selections for structural stability, and a database of structurally-tolerated sequences was compiled from the sequences of approximately 1000 unique clones. The results reveal that all four loops accommodate significantly greater diversity than is observed in nature. Thus, it appears that most sequence biases in the natural immune repertoire arise from factors other than structural constraints and, consequently, it should be possible to enhance the functions of antibodies significantly through in vitro evolution.
-
===Convergent solutions to VHH domain stabilization from natural and in vitro evolution===
+
A structure-based database of antibody variable domain diversity.,Bond CJ, Wiesmann C, Marsters JC Jr, Sidhu SS J Mol Biol. 2005 May 6;348(3):699-709. PMID:15826665<ref>PMID:15826665</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1shm" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15826665}}, adds the Publication Abstract to the page
+
*[[Antibody 3D structures|Antibody 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15826665 is the PubMed ID number.
+
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-
-->
+
== References ==
-
{{ABSTRACT_PUBMED_15826665}}
+
<references/>
-
 
+
__TOC__
-
==About this Structure==
+
</StructureSection>
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHM OCA].
+
[[Category: Lama glama]]
-
 
+
[[Category: Large Structures]]
-
==Reference==
+
[[Category: Bond CJ]]
-
A structure-based database of antibody variable domain diversity., Bond CJ, Wiesmann C, Marsters JC Jr, Sidhu SS, J Mol Biol. 2005 May 6;348(3):699-709. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15826665 15826665]
+
[[Category: Marsters JC]]
-
[[Category: Bond, C J.]]
+
[[Category: Sidhu SS]]
-
[[Category: Marsters, J C.]]
+
[[Category: Wiesmann C]]
-
[[Category: Sidhu, S S.]]
+
-
[[Category: Wiesmann, C.]]
+
-
[[Category: Heavy chain variable domain]]
+
-
[[Category: Immunoglobulin]]
+
-
[[Category: Vhh domain]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:18:08 2008''
+

Current revision

Convergent solutions to VHH domain stabilization from natural and in vitro evolution

PDB ID 1shm

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/1shm"
Personal tools