1mel

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{{STRUCTURE_1mel| PDB=1mel | SCENE= }}
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'''CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME'''
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===CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME===
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==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.
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==About this Structure==
==About this Structure==
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[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: Camel single-domain anti-lysozyme]]
[[Category: Camel single-domain anti-lysozyme]]
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Revision as of 20:48, 2 July 2008


PDB ID 1mel

Drag the structure with the mouse to rotate
1mel, resolution 2.50Å ()
Gene: ANTIBODY VH FRAGMENT CAB-LYS3 (Camelus dromedarius), ANTIBODY VH FRAGMENT CAB-LYS3 (Gallus gallus)
Activity: Lysozyme, with EC number 3.2.1.17
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme., Desmyter A, Transue TR, Ghahroudi MA, Thi MH, Poortmans F, Hamers R, Muyldermans S, Wyns L, Nat Struct Biol. 1996 Sep;3(9):803-11. PMID:8784355

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1MEL is a Single protein structure of sequence from Camelus dromedarius and Gallus gallus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme., Desmyter A, Transue TR, Ghahroudi MA, Thi MH, Poortmans F, Hamers R, Muyldermans S, Wyns L, Nat Struct Biol. 1996 Sep;3(9):803-11. PMID:8784355

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