Conserved Protein Domain Family
Transthyretin_like

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cd05469: Transthyretin_like 
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Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family which includes transthyretin (TTR) and a transthyretin-related protein called 5-hydroxyisourate hydrolase (HIUase). TTR and HIUase are homotetrameric proteins with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits. TTR transports thyroid hormones and retinol in the blood serum of vertebrates while HIUase catalyzes the second step in a three-step ureide pathway. TTRs are highly conserved and found only in vertebrates while the HIUases are found in a wide range of bacterial, plant, fungal, slime mold and vertebrate organisms.
Statistics
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PSSM-Id: 100112
View PSSM: cd05469
Aligned: 6 rows
Threshold Bit Score: 158.469
Threshold Setting Gi: 110590489
Created: 31-Jul-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitehomotetramer
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1KGJ_A; Rattus norvegicus transthyretin binds 3', 5'-dibromoflavone. Contacts determined at 3.5 Angstroms.
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  • Structure:1SN5_D; Sparus aurata transthyretin binds triiodothyronine. Contacts determined at 5 Angstroms.
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  • Structure:1IE4_A; Rattus norvegicus transthyretin binds two molecules of thyroxine; this homotetrameric thyretin structure contains two independent binding sites within the central core of the tetramer, each formed by a pair of monomers. Contacts determined at 3.5 Angstroms.
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  • Structure:1TYR_A; Homo sapiens transthyretin binds retinol. Contacts determined at 3.5 Angstroms.
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  • Citation:PMID 8536704
  • Structure:2H0F_A; Bacillus subtilis HIUase binds 8-azaxanthine (AZX). Contacts determined at 3.5 Angstroms.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                      10        20        30        40        50        60        70        80
              ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          # #                                     #                                  
1KGJ_A     10 CPLMVKVLDAVRGSPAVDVAVKVFKKtadgs-wepfASGKTAESGELHgltt-dekFTEGVYRVELDTKSYWkalg---- 83
1TYR_A     10 CPLMVKVLDAVRGSPAINVAVHVFRKaaddt-wepfASGKTSESGELHgltt-eeeFVEGIYKVEIDTKSYWkalg---- 83
1IE4_A     10 CPLMVKVLDAVRGSPAVDVAVKVFKKtadgs-wepfASGKTAESGELHgltt-dekFTEGVYRVELDTKSYWkalg---- 83
1SN5_D     13 CPLMVKILDAVKGTPAGSVALKVSQKtadgg-wtqiATGVTDATGEIHnlit-eqqFPAGVYRVEFDTKAYWtnqg---- 86
2H1X_A      7 SPLSTHVLNIAQGVPGANMTIVLHRLdpvssawnilTTGITNDDGRCPglit-kenFIAGVYKMRFETGKYWdalg---- 81
2H0F_A      9 GKLTTHILDLTCGKPAANVKIGLKRLges-----ixKEVYTNNDGRVDvpllageeLXSGEYVXEFHAGDYFasknxnaa 83
                      90       100       110
              ....*....|....*....|....*....|....*....
Feature 1                           # # #      # #   
1KGJ_A     84 ispFHEYAEVVFTAndsghrHYTIAALLSPYSYSTTAVV 122
1TYR_A     84 ispFHEHAEVVFTAndsgprRYTIAALLSPYSYSTTAVV 122
1IE4_A     84 ispFHEYAEVVFTAndsghrHYTIAALLSPYSYSTTAVV 122
1SN5_D     87 stpFHEVAEVVFDAhpeghrHYTLALLLSPFSYTTTAVV 125
2H1X_A     82 etcFYPYVEIVFTItnt-sqHYHVPLLLSRFSYSTYRGS 119
2H0F_A     84 dqpFLTIVTVRFQLadp-daHYHIPLLLSPFGYQVYRGS 121

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