1KTE,1B4Q,1EGO,1EGR,1FOV,1NM3,1QFN,1T1V,1WIK,3GRX,1J0F,1SJ6,1WRY,1JHB


Conserved Protein Domain Family
GRX_family
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cd02066: GRX_family 
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Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Links
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Statistics
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PSSM-Id: 239017
Aligned: 237 rows
Threshold Bit Score: 43.2246
Created: 12-Dec-2003
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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GSH bindingcatalytic
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:GSH binding site [chemical binding site]
Evidence:
  • Structure:3GRX; Escherichia coli GRX3 with bound GSH; contacts at 3.5A
  • Structure:1B4Q; Human GRX with bound GSH; contacts at 3.5A
  • Citation:PMID 9973569
  • Citation:PMID 9860827
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1           #        ###                                                     ##       
1KTE       13 KVVVFIKPt------CPFCRKTQELLSqlpfkeglLEFVDITatsdtneiqdYLQQLTga----------rTVPRVFIGK 76  pig
3GRX        2 NVEIYTKEt------CPYSHRAKALLSskg---vsFQELPIDgnaa---kreEMIKRSgr----------tTVPQIFIDA 59  Escherichia coli
CAB85507  238 SVVIYITTlrgirktFEDCNVVRSILDshe---vrFSERDVSmhsv---fkeEIRGIMgtk--------hvKIPAVFVKG 303 thale cress
BAB08969   90 SVVFYTTGlrsvrktFEACRRVRFLLEnhq---vmYRERDVSmdse---freEMWRLLgg---------kvTSPRLFIRG 154 thale cress
NP_497453  73 GVIVYLTScgvlrrsYDRCKNVTQLLEafr---vkYEIRDLNisnf---hvaELAEKLklnvefqkdlifdSLPLIYVDG 146 nematode
BAC42628  257 SVVFYTTTlrgirktFDDCNMIRFLLDsfk---vkYYERDVSmhre---yreELRRISaae-------tevLPPVLFVKG 323 thale cress
XP_426341 181 RIVIYTTSlrvvrttFERCELVRKIFQnhr---vkFEEKNIAlnsd---ygkELDERCrrvc------eapSLPVVFIDG 248 chicken
XP_463783 128 GVLLYTTTlrgvratFEACNAVRAALHshg---vaFRERDISmdrg---freELRHRIsldhh----drapLVPRLFVRG 197 Japanese rice
XP_371694 138 RVVIYTTClrvvrttFERCELVRKIFQnhr---vkFEEKNIAlnge---ygkELDERCrrvs------eapSLPVVFIDG 205 human
AAU89202  174 AVVLYTTSlrgvrktFEDCATVRRLLEglr---vaFLERDVSmhap---yrdELRALLvgld------daaVPPRLFVDG 241 Japanese rice

Feature 1                   
1KTE       77 ECIGGCTDLESMHK 90  pig
3GRX       60 QHIGGYDDLYALDA 73  Escherichia coli
CAB85507  304 RMVGSVEEVMRLEE 317 thale cress
BAB08969  155 RYIGGAEEVVALNE 168 thale cress
NP_497453 147 YFLGNEKTIVELND 160 nematode
BAC42628  324 RCIGGAQRVLGLHE 337 thale cress
XP_426341 249 HYLGGAEKILLMNE 262 chicken
XP_463783 198 NHVGGAAEVARLEE 211 Japanese rice
XP_371694 206 HYLGGAEKILSMNE 219 human
AAU89202  242 RYLGGANEVVTLHE 255 Japanese rice

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