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PDBsum entry 4oy9
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Cell adhesion
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PDB id
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4oy9
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References listed in PDB file
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Key reference
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Title
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The X-Ray structure of human p-Cadherin EC1-Ec2 in a closed conformation provides insight into the type i cadherin dimerization pathway.
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Authors
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A.Dalle vedove,
A.P.Lucarelli,
V.Nardone,
A.Matino,
E.Parisini.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2015,
71,
371-380.
[DOI no: ]
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PubMed id
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Abstract
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Cadherins are a large family of calcium-dependent proteins that mediate cellular
adherens junction formation and tissue morphogenesis. To date, the most studied
cadherins are those classified as classical, which are further divided into type
I or type II depending on selected sequence features. Unlike other members of
the classical cadherin family, a detailed structural characterization of
P-cadherin has not yet been fully obtained. Here, the high-resolution crystal
structure determination of the closed form of human P-cadherin EC1-EC2 is
reported. The structure shows a novel, monomeric packing arrangement that
provides a further snapshot in the yet-to-be-achieved complete description of
the highly dynamic cadherin dimerization pathway. Moreover, this is the first
multidomain cadherin fragment to be crystallized and structurally characterized
in its closed conformation that does not carry any extra N-terminal residues
before the naturally occurring aspartic acid at position 1. Finally, two clear
alternate conformations are observed for the critical Trp2 residue, suggestive
of a transient, metastable state. The P-cadherin structure and packing
arrangement shown here provide new and valuable information towards the complete
structural characterization of the still largely elusive cadherin dimerization
pathway.
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