Summary: Haemolymph juvenile hormone binding protein (JHBP)
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This is the Wikipedia entry entitled "Haemolymph juvenile hormone-binding protein". More...
Haemolymph juvenile hormone-binding protein Edit Wikipedia article
Haemolymph juvenile hormone-binding protein | |||||||||
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Identifiers | |||||||||
Symbol | JHBP | ||||||||
Pfam | PF06585 | ||||||||
InterPro | IPR010562 | ||||||||
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In molecular biology, the haemolymph juvenile hormone-binding protein (JHPB) family of proteins consists of several insect specific haemolymph juvenile hormone binding proteins. Juvenile hormone (JH) has a profound effect on insects. It regulates embryogenesis, maintains the status quo of larva development and stimulates reproductive maturation in the adult forms. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph.[1] The crystal structure of the JHBP from Galleria mellonella (greater wax moth) shows an unusual fold consisting of a long alpha-helix wrapped in a much curved antiparallel beta-sheet. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organisation of the major cavity and a disulfide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance.[2][3]
References
- ^ Kolodziejczyk R, Kochman M, Bujacz G, Dobryszycki P, Ozyhar A, Jaskolski M (March 2003). "Crystallization and preliminary crystallographic studies of juvenile hormone-binding protein from Galleria mellonella haemolymph". Acta Crystallogr. D. 59 (Pt 3): 519–21. doi:10.1107/S0907444902022904. PMID 12595713.
- ^ Kolodziejczyk R, Bujacz G, Jakob M, Ozyhar A, Jaskolski M, Kochman M (March 2008). "Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins". J. Mol. Biol. 377 (3): 870–81. doi:10.1016/j.jmb.2008.01.026. PMID 18291417.
- ^ Palli SR, Touhara K, Charles JP, Bonning BC, Atkinson JK, Trowell SC, Hiruma K, Goodman WG, Kyriakides T, Prestwich GD (June 1994). "A nuclear juvenile hormone-binding protein from larvae of Manduca sexta: a putative receptor for the metamorphic action of juvenile hormone". Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6191–5. doi:10.1073/pnas.91.13.6191. PMC 44164. PMID 8016136.
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Haemolymph juvenile hormone binding protein (JHBP) Provide feedback
This family consists of several insect-specific haemolymph juvenile hormone binding proteins (JHBP). Juvenile hormone regulates embryogenesis, maintains the status quo of larval development and stimulates reproductive maturation in the adult insect. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph [1]. The crystal structure of the JHBP from Galleria mellonella shows an unusual fold consisting of a long alpha-helix wrapped in a much curved antiparallel beta-sheet. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organisation of the major cavity and a disulfide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance [1]. This family now includes DUF233, PF03027.
Literature references
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Kolodziejczyk R, Kochman M, Bujacz G, Dobryszycki P, Ozyhar A, Jaskolski M; , Acta Crystallogr D Biol Crystallogr 2003;59:519-521.: Crystallization and preliminary crystallographic studies of juvenile hormone-binding protein from Galleria mellonella haemolymph. PUBMED:12595713 EPMC:12595713
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Kolodziejczyk R, Bujacz G, Jakob M, Ozyhar A, Jaskolski M, Kochman M;, J Mol Biol. 2008;377:870-881.: Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins. PUBMED:18291417 EPMC:18291417
This tab holds annotation information from the InterPro database.
InterPro entry IPR010562
This family consists of several insect specific haemolymph juvenile hormone binding proteins (JHBP). Juvenile hormone (JH) has a profound effect on insects. It regulates embryogenesis, maintains the status quo of larva development and stimulates reproductive maturation in the adult forms. JH is transported from the sites of its synthesis to target tissues by a haemolymph carrier called juvenile hormone-binding protein (JHBP). JHBP protects the JH molecules from hydrolysis by non-specific esterases present in the insect haemolymph [PUBMED:12595713]. The crystal structure of the JHBP from Galleria mellonella (Wax moth) shows an unusual fold consisting of a long alpha-helix wrapped in a much curved antiparallel beta-sheet. The folding pattern for this structure closely resembles that found in some tandem-repeat mammalian lipid-binding and bactericidal permeability-increasing proteins, with a similar organisation of the major cavity and a disulphide bond linking the long helix and the beta-sheet. It would appear that JHBP forms two cavities, only one of which, the one near the N- and C-termini, binds the hormone; binding induces a conformational change, of unknown significance [PUBMED:18291417, PUBMED:8016136].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Aha1_BPI (CL0648), which has the following description:
This superfamily was defined based on the ECOD resource which combines two SCOP superfamilies.
The clan contains the following 8 members:
Aha1_N DUF1439 Grp7_allergen JHBP LBP_BPI_CETP LBP_BPI_CETP_C SMP_C2CD2L SMP_LBDAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (232) |
Full (2529) |
Representative proteomes | UniProt (4385) |
NCBI (6512) |
Meta (0) |
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RP15 (530) |
RP35 (1111) |
RP55 (1765) |
RP75 (2461) |
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PP/heatmap | 1 |
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Seed (232) |
Full (2529) |
Representative proteomes | UniProt (4385) |
NCBI (6512) |
Meta (0) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (530) |
RP35 (1111) |
RP55 (1765) |
RP75 (2461) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
Seed source: | Pfam-B_19686 (release 10.0) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Moxon SJ |
Number in seed: | 232 |
Number in full: | 2529 |
Average length of the domain: | 210.80 aa |
Average identity of full alignment: | 18 % |
Average coverage of the sequence by the domain: | 84.23 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 239 | ||||||||||||
Family (HMM) version: | 12 | ||||||||||||
Download: | download the raw HMM for this family |
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Interactions
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JHBPStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the JHBP domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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