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PDBsum entry 3tw8
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Protein transport
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PDB id
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3tw8
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Contents |
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343 a.a.
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169 a.a.
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362 a.a.
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PDB id:
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| Name: |
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Protein transport
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Title:
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Gef domain of dennd 1b in complex with rab gtpase rab35
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Structure:
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Denn domain-containing protein 1b. Chain: a, c. Fragment: unp residues 1-391. Synonym: connecdenn 2, protein fam31b. Engineered: yes. Ras-related protein rab-35. Chain: b, d. Fragment: unp residues 1-180. Synonym: gtp-binding protein ray, ras-related protein rab-1c.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: dennd1b, c1orf218, fam31b. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: rab35, rab1c, ray.
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Resolution:
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2.10Å
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R-factor:
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0.230
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R-free:
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0.269
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Authors:
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X.D.Wu,D.Kummel,K.M.Reinisch
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Key ref:
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X.Wu
et al.
(2011).
Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate.
Proc Natl Acad Sci U S A,
108,
18672-18677.
PubMed id:
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Date:
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21-Sep-11
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Release date:
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16-Nov-11
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PROCHECK
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Headers
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References
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Q6P3S1
(DEN1B_HUMAN) -
DENN domain-containing protein 1B from Homo sapiens
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Seq:
Struc:
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775 a.a.
343 a.a.
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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Proc Natl Acad Sci U S A
108:18672-18677
(2011)
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PubMed id:
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Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate.
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X.Wu,
M.J.Bradley,
Y.Cai,
D.Kümmel,
E.M.De La Cruz,
F.A.Barr,
K.M.Reinisch.
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ABSTRACT
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Rab GTPases are key regulators of membrane traffic pathways within eukaryotic
cells. They are specifically activated by guanine nucleotide exchange factors
(GEFs), which convert them from their "inactive" GDP-bound form to the
"active" GTP-bound form. In higher eukaryotes, proteins containing
DENN-domains comprise a major GEF family. Here we describe at 2.1-Å resolution
the first structure of a DENN-domain protein, DENND1B-S, complexed with its
substrate Rab35, providing novel insights as to how DENN-domain GEFs interact
with and activate Rabs. DENND1B-S is bi-lobed, and interactions with Rab35 are
through conserved surfaces in both lobes. Rab35 binds via switch regions I and
II, around the nucleotide-binding pocket. Positional shifts in Rab residues
required for nucleotide binding may lower its affinity for bound GDP, and a
conformational change in switch I, which makes the nucleotide-binding pocket
more solvent accessible, likely also facilitates exchange.
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Links
