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PDBsum entry 5e4k
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Sugar binding protein
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PDB id
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5e4k
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References listed in PDB file
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Key reference
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Title
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Crystal structures of the ligand-Binding region of uparap: effect of calcium ion binding.
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Authors
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C.Yuan,
H.J.Jürgensen,
L.H.Engelholm,
R.Li,
M.Liu,
L.Jiang,
Z.Luo,
N.Behrendt,
M.Huang.
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Ref.
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Biochem J, 2016,
473,
2359-2368.
[DOI no: ]
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PubMed id
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Abstract
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The proteins of the mannose receptor (MR) family share a common domain
organization and have a broad range of biological functions. Urokinase
plasminogen activator receptor-associated protein (uPARAP) (or Endo180) is a
member of this family and plays an important role in extracellular matrix
remodelling through interaction with its ligands, including collagens and
urokinase plasminogen activator receptor (uPAR). We report the crystal
structures of the first four domains of uPARAP (also named the ligand-binding
region, LBR) at pH 7.4 in Ca(2+)-bound and Ca(2+)-free forms. The first domain
(cysteine-rich or CysR domain) folds into a new and unique conformation
different from the β-trefoil fold of typical CysR domains. The so-called long
loop regions (LLRs) of the C-type lectin-like domain (CTLD) 1 and 2 (the third
and fourth domain) mediate the direct contacts between these domains. These LLRs
undergo a Ca(2+)-dependent conformational change, and this is likely to be the
key structural determinant affecting the overall conformation of uPARAP. Our
results provide a molecular mechanism to support the structural flexibility of
uPARAP, and shed light on the structural flexibility of other members of the MR
family.
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