1FRG	Viral Protein Immune System	date	Jan 17, 1994
title	Crystal Structure, Sequence, And Epitope Mapping Of A Peptide Complex Of An Anti-Influenza Ha Peptide Antibody Fab 26(Slash)9: Fine-Tuning Antibody Specificity
authors	M.E.A.Churchill, I.A.Wilson
compound		source
Molecule: Igg2a 269 Fab (Light Chain) Chain: L Engineered: Yes Molecule: Igg2a 269 Fab (Heavy Chain) Chain: H Engineered: Yes Molecule: Influenza Hemagglutinin Ha1 (Strain X47) (Residues 101 - 108); Chain: P Engineered: Yes
symmetry	Space Group: P 21 21 21	R_factor 0.190 R_Free NULL
crystal cell	length a length b length c angle alpha angle beta angle gamma 66.600 115.100 73.300 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2 Å
ligand	ACE, NH2	enzyme
related structures	by homologous chain: 1A5F, 1CLZ, 1GGC, 1GGI
similarity	Belongs to the influenza viruses Hemagglutinin family.
subunit	Homotrimer of disulfide-linked ha1-ha2.
post-translat. modifications	Palmitoylated (by similarity). In natural infection, inactive ha is matured into ha1 and ha2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is tryptase clara.
subcellular loc.	Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. Type i membrane protein. Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain.
function	Plays a major role in the determination of host range restriction and virulence. Class i viral fusion protein. Several trimers are required to form a competent fusion pore. Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Low ph in endosomes induce an irreversible conformational change in ha2, releasing the fusion hydrophobic peptide. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane.
Gene Ontology	Chain Function Process Component P host cell surface receptor b... viral envelope fusion with h... plasma membrane membrane integral to membrane virion viral envelope host cell plasma membrane virion membrane
Primary reference	Crystal structure of a peptide complex of anti-influenza peptide antibody Fab 26/9. Comparison of two different antibodies bound to the same peptide antigen., Churchill ME, Stura EA, Pinilla C, Appel JR, Houghten RA, Kono DH, Balderas RS, Fieser GG, Schulze-Gahmen U, Wilson IA, J Mol Biol 1994 Aug 26;241(4):534-56. PMID:7520084

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (76 Kb) [Save to disk] Biological Unit Coordinates (1frg.pdb1.gz) 71 Kb CSU: Contacts of Structural Units for 1FRG Likely Quarternary Molecular Structure file(s) for 1FRG Structure Factors (126 Kb) Retrieve 1FRG in mmCIF format [Save to disk]

View 1FRG in 3D

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Visual 3D analysis of 1FRG

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Structure-derived information

Electron Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1FRG, from MSDmotif at EBI Genome occurence of 1FRG's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1frgh1, region H:218-336 [Jmol] [rasmolscript] [script source]     - Domain d1frgh2, region H:337-437 [Jmol] [rasmolscript] [script source]     - Domain d1frgl1, region L:1-113 [Jmol] [rasmolscript] [script source]     - Domain d1frgl2, region L:114-217 [Jmol] [rasmolscript] [script source] Fold representative 1frg from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1frg_H] [1frg_P] [1frg_L]

Other resources with information on 1FRG

InterPro: IPR001364 , IPR000149 MMDB (Entrez's Structure Database)

Movements, Movies and Images

Domain movements in 1FRG from the Database of Macromolecular Movements. Images from IMB Jena Image Library of Biological Macromolecules.

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