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PDBsum entry 5d68
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Signaling protein
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PDB id
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5d68
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References listed in PDB file
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Key reference
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Title
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Structural analysis of the krit1 ankyrin repeat and ferm domains reveals a conformationally stable ard-Ferm interface.
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Authors
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R.Zhang,
X.Li,
T.J.Boggon.
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Ref.
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J Struct Biol, 2015,
192,
449-456.
[DOI no: ]
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PubMed id
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Abstract
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Cerebral cavernous malformations (CCM) are vascular dysplasias that usually
occur in the brain and are associated with mutations in the KRIT1/CCM1,
CCM2/MGC4607/OSM/Malcavernin, and PDCD10/CCM3/TFAR15 genes. Here we report the
2.9Å crystal structure of the ankyrin repeat domain (ARD) and FERM domain of
the protein product of KRIT1 (KRIT1; Krev interaction trapped 1). The crystal
structure reveals that the KRIT1 ARD contains 4 ankyrin repeats. There is an
unusual conformation in the ANK4 repeat that is stabilized by Trp-404, and the
structure reveals a solvent exposed ankyrin groove. Domain orientations of the
three copies within the asymmetric unit suggest a stable interaction between
KRIT1 ARD and FERM domains, indicating a globular ARD-FERM module. This
resembles the additional F0 domain found N-terminal to the FERM domain of talin.
Structural analysis of KRIT1 ARD-FERM highlights surface regions of high
evolutionary conservation, and suggests potential sites that could mediate
interaction with binding partners. The structure therefore provides a better
understanding of KRIT1 at the molecular level.
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