1mel: Difference between revisions

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[[Image:1mel.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME~~'''~~

===CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME===

~~==Overview==~~

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The ~~Camelidae is~~ the ~~only taxonomic family known~~ to ~~possess functional heavy-chain antibodies, lacking light chains. We report here~~ the 2.~~5 A resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mouse VH domains, there are no major backbone rearrangements in the VH framework~~. ~~However~~, ~~the architecture of the region of VH that interacts with a VL in a conventional FV~~ is ~~different from any previously seen. Moreover, the CDR1 region, although in sequence homologous to human CDR1, deviates fundamentally from~~ the canonical structure. Additionally, one half of the CDR3 contacts the VH region which in conventional immunoglobulins interacts with a VL whereas the other half protrudes from the antigen binding site and penetrates deeply into the active site of lysozyme.

The line below this paragraph, {{ABSTRACT_PUBMED_8784355}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8784355 is the PubMed ID number.

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==About this Structure==

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[[Category: Wyns, L.]]

[[Category: Camel single-domain anti-lysozyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:56:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:48:06 2008''

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-[[Image:1mel.jpg|left|200px]]
+{{Seed}}
+[[Image:1mel.png|left|200px]]
 <!--
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 {{STRUCTURE_1mel|  PDB=1mel  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME'''
+===CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME===
-==Overview==
+<!--
-The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies, lacking light chains. We report here the 2.5 A resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mouse VH domains, there are no major backbone rearrangements in the VH framework. However, the architecture of the region of VH that interacts with a VL in a conventional FV is different from any previously seen. Moreover, the CDR1 region, although in sequence homologous to human CDR1, deviates fundamentally from the canonical structure. Additionally, one half of the CDR3 contacts the VH region which in conventional immunoglobulins interacts with a VL whereas the other half protrudes from the antigen binding site and penetrates deeply into the active site of lysozyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_8784355}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8784355 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8784355}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Wyns, L.]]
 [[Category: Camel single-domain anti-lysozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:56:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:48:06 2008''