1XZ0,1A1M,1ZAG,1JE6,1N5A


Conserved Protein Domain Family
IgC_MHC_I_alpha3

?
cd07698: IgC_MHC_I_alpha3 
Click on image for an interactive view with Cn3D
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain
IgC_MHC_I_alpha3; Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta2 microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.
Statistics
?
PSSM-Id: 143322
View PSSM: cd07698
Aligned: 26 rows
Threshold Bit Score: 109.685
Threshold Setting Gi: 6525049
Created: 17-Oct-2008
Updated: 18-Aug-2016
Structure
?
Program:
Drawing:
Aligned Rows:
 
heterodimerMHC binding
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:heterodimer interface [polypeptide binding site]
Evidence:
  • Structure:1A1M_A; human MHC class I alpha3 domain forms dimer with beta2 microglobulin, defined using 3.5 A contacts
    View structure with Cn3D
  • Citation:PMID 8624812
  • Structure:1N5A_A; muring MHC class I alpha3 domain forms dimer with beta2 microglobulin, defined using 3.5 A contacts.
    View structure with Cn3D

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                           # #                           ## ###     # #                
1XZ0_A      185 VKPEAWLSHgpspgpghLQLVCHVSGFYPKPVWVMWMrge--qeqQGTQRGDILPSADGTWYLRATLEVaag---eaaDL 259
1A1M_A      183 DPPKTHVTHhpvs-dheATLRCWALGFYPAEITLTWQrdge-dqtQDTELVETRPAGDRTFQKWAAVVVpsg---eeqRY 257
1N5A_A      183 DSPKAHVTHhprs-kgeVTLRCWALGFYPADITLTWQlnge-eltQDMELVETRPAGDGTFQKWASVVVplg---keqNY 257
gi 210887   148 EPPKIKVTSradh-dnmETLICRADGFYPKDIHPVWIrdge-vweQETMRGLMAPNVDGTFHTWIGIKIdpk---drgRF 222
gi 122152   202 ERPEVRVWGkea--dgiLTLSCRAHGFYPRPIVVSWLkdga-vrgQDAHSGGIVPNGDGTYHTWVTIDAqpg---dgdKY 275
gi 4504417  202 EPPLVRVNRketf-pgvTALFCKAHGFYPPEIYMTWMknge-eivQEIDYGDILPSGDGTYQAWASIELdpq---ssnLY 276
gi 6624732  209 VPPAVTVTCsqal-egtDNLTCQAISFSPQNISVAWYqdekavspDTQQSGGVLPDGNGTYRTWVTLRVpqg---eeqRF 284
gi 26788069 197 VSPQVSLLQks----ssSPVVCHATGFYPSGIKISWQkngq-dhdEDVELEELLPNEDGTFQKSSTLTVtpee-wknnKF 270
gi 2995931  205 VPPTASVFQeee---ssPEVVCHATGFFPKTVMITWQkdge-dvhEDVELRETLPNQDGTFQKRSILTVsaed-lqkhTY 279
gi 976114   184 DLPSVSLLQks----psSPITCHATGFYPDKAEMFWRksge-elhEHVEKGEIVPNNDGSFQMDVKLAHpsiesedwtNY 258
                        90       100
                ....*....|....*....|
Feature 1                           
1XZ0_A      260 SCRVKHSsle-gqDIVLYWV 278
1A1M_A      258 TCHVQHEgl--pkPLTLRWE 275
1N5A_A      258 TCRVYHEgl--pePLTLRWE 275
gi 210887   223 QCRVDHAglekpvDLAVEEP 242
gi 122152   276 QCRVEHAsl--pqPGLYSWE 293
gi 4504417  277 SCHVEHCgv--hmVLQVPQE 294
gi 6624732  285 SCHVEHGgn--hsVHAVPCA 302
gi 26788069 271 RCVVEHQgktkteKEIRTNE 290
gi 2995931  280 TCVIQHSsl--ekEMVLPVS 297
gi 976114   259 ECVFQLYgk---kDIITKLE 275

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap