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PDBsum entry 2brs
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* Residue conservation analysis
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PDB id:
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Lectin
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Title:
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Embp heparin complex
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Structure:
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Eosinophil-granule major basic protein. Chain: a, b. Synonym: mbp, embp, pregnancy associated major basic protein, proteoglycan 2 bone marrow, bmpg. Other_details: heparin sulphate
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Cell: eosinophil
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Resolution:
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2.20Å
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R-factor:
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0.247
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R-free:
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0.291
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Authors:
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G.J.Swaminathan,D.G.Myszka,P.S.Katsamba,L.E.Ohnuki,G.J.Gleich, K.R.Acharya
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Key ref:
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G.J.Swaminathan
et al.
(2005).
Eosinophil-granule major basic protein, a C-type lectin, binds heparin.
Biochemistry,
44,
14152-14158.
PubMed id:
DOI:
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Date:
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11-May-05
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Release date:
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26-Oct-05
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PROCHECK
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Headers
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References
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P13727
(PRG2_HUMAN) -
Bone marrow proteoglycan from Homo sapiens
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Seq:
Struc:
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222 a.a.
115 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Biochemistry
44:14152-14158
(2005)
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PubMed id:
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Eosinophil-granule major basic protein, a C-type lectin, binds heparin.
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G.J.Swaminathan,
D.G.Myszka,
P.S.Katsamba,
L.E.Ohnuki,
G.J.Gleich,
K.R.Acharya.
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ABSTRACT
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The eosinophil major basic protein (EMBP), a constituent of the eosinophil
secondary granule, is implicated in cytotoxicity and mediation of allergic
disorders such as asthma. It is a member of the C-type lectin family, but lacks
a Ca(2+)- and carbohydrate-binding site as seen in other members of this family.
Here, we report the crystal structure of EMBP in complex with a heparin
disaccharide and in the absence of Ca(2+), the first such report of any C-lectin
with this sugar. We also provide direct evidence of binding of EMBP to heparin
and heparin disaccharide by surface plasmon resonance. We propose that the
sugars recognized by EMBP are likely to be proteoglycans such as heparin,
leading to new interpretations for EMBP function.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Torrent,
M.V.Nogués,
and
E.Boix
(2011).
Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site.
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J Mol Recognit,
24,
90.
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R.D.Cummings
(2009).
The repertoire of glycan determinants in the human glycome.
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Mol Biosyst,
5,
1087-1104.
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L.A.Wagner,
L.E.Ohnuki,
K.Parsawar,
G.J.Gleich,
and
C.C.Nelson
(2007).
Human eosinophil major basic protein 2: location of disulfide bonds and free sulfhydryl groups.
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Protein J,
26,
13-18.
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R.L.Rich,
and
D.G.Myszka
(2006).
Survey of the year 2005 commercial optical biosensor literature.
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J Mol Recognit,
19,
478-534.
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S.Glerup,
S.Kløverpris,
and
C.Oxvig
(2006).
The proform of the eosinophil major basic protein binds the cell surface through a site distinct from its C-type lectin ligand-binding region.
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J Biol Chem,
281,
31509-31516.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
