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.


1a14

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a14.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a14.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a14| PDB=1a14 | SCENE= }}
{{STRUCTURE_1a14| PDB=1a14 | SCENE= }}
-
'''COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE'''
+
===COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE===
-
==Overview==
+
<!--
-
The structure of the complex between a recombinant single-chain Fv construct of antibody NC10 with a five-residue peptide linker between VH and VL (termed scFv(5)), and its antigen, tetrameric neuraminidase from influenza virus (NA), has been determined and refined at 2.5 A resolution. The antibody-antigen binding interface is very similar to that of a similar NC10 scFv-NA complex in which the scFv has a 15-residue peptide linker (scFv(15)), and the NC10 Fab-NA complex. However, scFv(5) and scFv(15) have different stoichiometries in solution. While scFv(15) is predominantly monomeric in solution, scFv(5) forms dimers exclusively, because the five-residue linker is not long enough to permit VH and VL domains from the same polypeptide associating and forming an antigen-binding site. Upon forming a complex with NA, scFv(15) forms a approximately 300 kDa complex corresponding to one NA tetramer binding four scFv(15) monomers, while scFv(5) forms a approximately 590 kDa complex, corresponding to two NA tetramers crosslinked by four bivalent scFv(5) dimers. However, the dimeric scFv(5) in the scFv(5)-NA crystals does not crosslink NA tetramers, and modelling studies indicate that it is not possible to pack four dimeric and simultaneously bivalent scFvs between the NA tetramers with only a five-residue linker between VH and VL. The inability arises from the exacting requirement to orient the two antigen-binding surfaces to bind the tetrameric NA antigen while avoiding steric clashes with NC10 scFv(5) dimers bound to other sites on the NA tetramer. The utility of bivalent or bifunctional scFvs with short linkers may therefore be restricted by the steric constraints imposed by binding multivalent antigens.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9642070}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9642070 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9642070}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Glycosylated protein]]
[[Category: Glycosylated protein]]
[[Category: Single-chain antibody]]
[[Category: Single-chain antibody]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:39:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:45:53 2008''

Revision as of 12:45, 30 June 2008

Image:1a14.png

Template:STRUCTURE 1a14

COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 5 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE

Template:ABSTRACT PUBMED 9642070

About this Structure

1A14 is a Protein complex structure of sequences from Influenza a virus and Mus musculus. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of single-chain Fv-neuraminidase complexes., Malby RL, McCoy AJ, Kortt AA, Hudson PJ, Colman PM, J Mol Biol. 1998 Jun 19;279(4):901-10. PMID:9642070

Page seeded by OCA on Mon Jun 30 15:45:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a14"
Personal tools