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1rjb

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1rjb, resolution 2.10Å ()

Activity:

Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2

Domains:

PTKc_PDGFR, S_TKc

Structural annotation:
Resources:	CATH : 1Rjba01, 1Rjba02 InterPro : Ipr013783, Ipr008266, Ipr013151, Ipr001824, Ipr001245, Ipr011009, Ipr007110, Ipr000719 Pfam : PF07714 SCOP : d1rjba_ UniProt : P36888

Functional annotation:
Resources:	GeneCard : FLT3
Cellular component:	integral to plasma membrane integral to membrane membrane
Biological process:	protein amino acid phosphorylation lymphocyte differentiation positive regulation of cell proliferation transmembrane receptor protein tyrosine kinase signaling pathway
Molecular function:	protein kinase activity protein binding kinase activity transmembrane receptor protein tyrosine kinase activity nucleotide binding protein-tyrosine kinase activity receptor activity transferase activity ATP binding vascular endothelial growth factor receptor activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal Structure of FLT3

Publication Abstract from PubMed

FLT3 is a type III receptor tyrosine kinase that is thought to play a key role in hematopoiesis. Certain classes of FLT3 mutations cause constitutively activated forms of the receptor that are found in significant numbers of patients with acute myelogenous leukemia (AML). The mutations occur either in the activation loop, for example, as point mutations of Asp835 or as internal tandem duplication (ITD) sequences in the juxtamembrane (JM) domain. To further understand the nature of FLT3 autoinhibition and regulation, we have determined the crystal structure of the autoinhibited form of FLT3. This structure shows the autoinhibitory conformation of a complete JM domain in this class of receptor tyrosine kinases. The detailed inhibitory mechanism of the JM domain is revealed, which is likely utilized by other members of type III receptor tyrosine kinases.

The structural basis for autoinhibition of FLT3 by the juxtamembrane domain., Griffith J, Black J, Faerman C, Swenson L, Wynn M, Lu F, Lippke J, Saxena K, Mol Cell. 2004 Jan 30;13(2):169-78. PMID:14759363

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1RJB is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Griffith J, Black J, Faerman C, Swenson L, Wynn M, Lu F, Lippke J, Saxena K. The structural basis for autoinhibition of FLT3 by the juxtamembrane domain. Mol Cell. 2004 Jan 30;13(2):169-78. PMID:14759363

Page seeded by OCA on Tue Feb 17 23:53:06 2009

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1rjb

From Proteopedia

Crystal Structure of FLT3

About this Structure

Reference

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