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PDBsum entry 3ddc
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Hydrolase/apoptosis
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PDB id
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3ddc
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References listed in PDB file
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Key reference
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Title
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Novel type of ras effector interaction established between tumour suppressor nore1a and ras switch ii.
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Authors
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B.Stieglitz,
C.Bee,
D.Schwarz,
O.Yildiz,
A.Moshnikova,
A.Khokhlatchev,
C.Herrmann.
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Ref.
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Embo J, 2008,
27,
1995-2005.
[DOI no: ]
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PubMed id
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Abstract
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A class of putative Ras effectors called Ras association domain family (RASSF)
represents non-enzymatic adaptors that were shown to be important in tumour
suppression. RASSF5, a member of this family, exists in two splice variants
known as NORE1A and RAPL. Both of them are involved in distinct cellular
pathways triggered by Ras and Rap, respectively. Here we describe the crystal
structure of Ras in complex with the Ras binding domain (RBD) of NORE1A/RAPL.
All Ras effectors share a common topology in their RBD creating an interface
with the switch I region of Ras, whereas NORE1A/RAPL RBD reveals additional
structural elements forming a unique Ras switch II binding site. Consequently,
the contact area of NORE1A is extended as compared with other Ras effectors. We
demonstrate that the enlarged interface provides a rationale for an
exceptionally long lifetime of the complex. This is a specific attribute
characterizing the effector function of NORE1A/RAPL as adaptors, in contrast to
classical enzymatic effectors such as Raf, RalGDS or PI3K, which are known to
form highly dynamic short-lived complexes with Ras.
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