PDBsum entry: 1far

Serine/threonine protein kinase

PDB-id: 1far

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

52 a.a. *

Metal ions

_ZN ×2

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1far

Name:

Serine/threonine protein kinase

Title:

Raf-1 cysteine rich domain, nmr, minimized average structure

Structure:

Raf-1. Chain: a. Fragment: cysteine-rich domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

P04049 (RAF1_HUMAN)

Seq:

Struc:

Seq:

Struc:

Seq:

648 a.a.

Struc:

52 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Enzyme class:

E.C.2.7.11.1   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

ATP + a protein = ADP + a phosphoprotein

Resolution:

not givenÅ

NMR structure:

1 models

Authors:

H.R.Mott,S.L.Campbell

Key ref:

H.R.Mott et al. (1996). The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site.. Proc Natl Acad Sci U S A, 93, 8312-8317. [PubMed id: 8710867] [DOI: 10.1073/pnas.93.16.8312]

Date:

05-Sep-96

Release date:

27-Jan-97

Related entries:

1faq

Quick_links

Procheck

Clefts

Surface

ProFunc

Key reference

DOI no: 10.1073/pnas.93.16.8312

Proc Natl Acad Sci U S A 93:8312-8317 (1996)

PubMed id: 8710867

The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site.

H.R.Mott, J.W.Carpenter, S.Zhong, S.Ghosh, R.M.Bell, S.L.Campbell.

ABSTRACT

The Raf-1 protein kinase is the best-characterized downstream effector of activated Ras. Interaction with Ras leads to Raf-1 activation and results in transduction of cell growth and differentiation signals. The details of Raf-1 activation are unclear, but our characterization of a second Ras-binding site in the cysteine-rich domain (CRD) and the involvement of both Ras-binding sites in effective Raf-1-mediated transformation provides insight into the molecular aspects and consequences of Ras-Raf interactions. The Raf-1 CRD is a member of an emerging family of domains, many of which are found within signal transducing proteins. Several contain binding sites for diacylglycerol (or phorbol esters) and phosphatidylserine and are believed to play a role in membrane translocation and enzyme activation. The CRD from Raf-1 does not bind diacylglycerol but interacts with Ras and phosphatidylserine. To investigate the ligand-binding specificities associated with CRDs, we have determined the solution structure of the Raf-1 CRD using heteronuclear multidimensional NMR. We show that there are differences between this structure and the structures of two related domains from protein kinase C (PKC). The differences are confined to regions of the CRDs involved in binding phorbol ester in the PKC domains. Since phosphatidylserine is a common ligand, we expect its binding site to be located in regions where the structures of the Raf-1 and PKC domains are similar. The structure of the Raf-1 CRD represents an example of this family of domains that does not bind diacylglycerol and provides a framework for investigating its interactions with other molecules.