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.


1hin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1hin" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hin, resolution 3.1&Aring;" /> '''STRUCTURAL EVIDENCE ...)
Current revision (11:32, 27 March 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hin.gif|left|200px]]<br />
 
-
<applet load="1hin" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1hin, resolution 3.1&Aring;" />
 
-
'''STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION'''<br />
 
-
==Overview==
+
==STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION==
-
The three-dimensional structure of a specific antibody (Fab 17/9) to a, peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two, independent crystal complexes of this antibody with bound peptide, (TyrP100-LeuP108) have been determined by x-ray crystallographic, techniques at 2.0 A, 2.9 A, and 3.1 A resolution, respectively. The, nonapeptide antigen assumes a type I beta turn in the antibody combining, site and interacts primarily with the Fab hypervariable loops L3, H2, and, H3. Comparison of the bound and unbound Fab structures shows that a major, rearrangement in the H3 loop accompanies antigen binding. This, conformational change results in the creation of a binding pocket for the, beta turn of the peptide, allowing TyrP105 to be accommodated. The, conformation of the peptide bound to the antibody shows similarity to its, cognate sequence in the HA1, suggesting a possible mechanism for the, cross-reactivity of this Fab with monomeric hemagglutinin. The structures, of the free and antigen bound antibodies demonstrate the flexibility of, the antibody combining site and provide an example of induced fit as a, mechanism for antibody-antigen recognition.
+
<StructureSection load='1hin' size='340' side='right'caption='[[1hin]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1hin]] is a 3 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=1HIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HIN FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=1hin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hin OCA], [https://pdbe.org/1hin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hin RCSB], [https://www.ebi.ac.uk/pdbsum/1hin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hin ProSAT]</span></td></tr>
 +
</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/hi/1hin_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=1hin ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1HIN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HIN OCA].
+
*[[Antibody 3D structures|Antibody 3D structures]]
-
 
+
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-
==Reference==
+
__TOC__
-
Structural evidence for induced fit as a mechanism for antibody-antigen recognition., Rini JM, Schulze-Gahmen U, Wilson IA, Science. 1992 Feb 21;255(5047):959-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1546293 1546293]
+
</StructureSection>
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Rini, J.M.]]
+
[[Category: Mus musculus]]
-
[[Category: Wilson, I.A.]]
+
[[Category: Rini JM]]
-
[[Category: immunoglobulin]]
+
[[Category: Wilson IA]]
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:32:12 2007''
+

Current revision

STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION

PDB ID 1hin

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/1hin"
Personal tools