3PMR


Conserved Protein Domain Family
APP_E2

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pfam12925: APP_E2 
E2 domain of amyloid precursor protein
The E2 domain is the largest of the conserved domains of the amyloid precursor protein. The structure of E2 consists of two coiled-coil sub-structures connected through a continuous helix, and bears an unexpected resemblance to the spectrin family of protein structures.E 2 can reversibly dimerize in solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. The high degree of conservation of residues at the putative dimer interface suggests that the E2 dimer observed in the crystal could be physiologically relevant. Heparin sulfate proteoglycans, the putative ligands for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.
Statistics
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PSSM-Id: 463752
Aligned: 17 rows
Threshold Bit Score: 217.597
Created: 24-Mar-2022
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
3PMR_A         5 TPTPRPTDGV-DIYFGMPG-EISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKAD-------RQALNEHFQ 75 
ADM32510     264 TTTAASTATS-DPYFSHFD-PRTEHQSYKDAQQRLEETHREKITKVMKEWSELEDRYQQMMTADpaaaqtfRQRMTAKFQ 341
XP_002426949 294 STPKSGPPTP-DPYFTHFD-PRIEHQAYKEAQLRLEELHREKVTKVMKDWSDLEERYQDMRTSDpkaaeefKKRMTQRFQ 371
EGI68173     248 QQPSQPQGTP-DPYLTHFD-PRSEHQSYKQAQMRLEEVHKEKVTKVMKDWSDLEERYQDIRAHDpvaadafKRWMTARFQ 325
XP_015791357 299 TTTTTTERPI-DHYLSHFD-SNHEHDSYKAAQKSLEESHRDKVTKVMKEWSELEERYQEMKLKDpkgaaefKRKMTSRFQ 376
EFX86398     208 vsPPKPSPTP-DPYLTHYN-PKKERDDFLDAEQRLEERHRERVTKIMKDWSELEDRYQDLHSTDakgaeefKHKMTNRFQ 285
CAP33080     229 kdegeeSSAQ-DPYFKIAN-WTNEHEDFKKAETRMDEKHRKRVEKVMKEWGDLETRYNEQKTKDpkgaekfKAQMNARFQ 306
ESO01307     218 PTSSKSADALlKGYLKDNQpRRNEHELFRKAESDMEKKHHEHIAKIMQDWALARQRVQELKNIDqkassklSKEVTSRFQ 297
1_pfamImport   1 TTAASTPDAV-DKYLETPG-DENEHSHFQKAKERLEAKHRERMSQVMREWEEAEHQAKNLPKAD-------KKAVIQHFQ 71 
EEN69130     245 VAPSPTPKAV-DPYFLEED-SDNEHKMFLEARKRVEEKHRLRMTQVMKQWEEAEERYQELKSKDpngaelmKKEMMERFQ 322
3PMR_A        76 SILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAAL--QADPPQAERVLLALRRYLRAEQKEQRHTLRHYQH 153
ADM32510     342 ANVQSLEEEGVSERRRLAALHQQRVLAHLAQRRRTALACYTRSL--KDTPPNAHRVQKCLQRLVRALAAERSGALAAWRR 419
XP_002426949 372 RTVQSLEDEGNAEKHQLVAMHQQRVMAHINQRKKEAMTCYTQAL--NENPPNAHRVQKCLQKLLRCLHKDRHHTIAHYKH 449
EGI68173     326 ETVAALEESGAAEKHQLSAMHQQRVQEAVKQRNEEAMSCYTAAL--NETPPNMHRIQKCLQKLLRALHKDRHHTIAHYKH 403
XP_015791357 377 KTVEALEEEGSAERRQLISMHQQRVMTVINMRKKAAMDCYTQSL--DQTPLKTKRIEKCLEKLLRALEKDRTHTLHHFRH 454
EFX86398     286 KLVKSMEDEDVMEKRQLSAVHQQRVLAAINEKKRDAMTCYTDAL--NENPANTHRIQKCLEKLLRALHKDRHHSISHFRH 363
CAP33080     307 KTVSSLEEEHKRMRKEIEAVHEERVQAVLNEKKRDATHDYRQALatHVNKPNKHSVLQSLKAYIRAEEKDRMHTLNRYRH 386
ESO01307     298 KTYEAEELEAEMEKMQLMDLHEQRVRKQFTDKQADLLEKFKKSL--HEKEPSTQHIRSALIHLLRLQQKYRLHLINRFRR 375
1_pfamImport  72 EKVESLEQEAANERQQLVETHMARVEAMLNDRRRVALENYITAL--QAVPPKVPHQFNTLMYISAKAVKDVTTTWQQNEE 149
EEN69130     323 VTVNALEQEGQSEREQLLQTHQQRVETMLNNKKRVAMEDYMDAL--GENPPHAHKILRALKAYIHAEQKDRLHSMRHFEH 400
3PMR_A       154 VAAV--DPEKAQQMRFQVHTHLQVIEERVNQSLGLL 187
ADM32510     420 AAAA--GREAASAERASAADRLQDADRALQRALSSL 453
XP_002426949 450 LLSS--SFEQAEREKSITLEHLTDIDRMVNQSLQML 483
EGI68173     404 LLDS--SLEQAQREKPATLEHLAEIDRITNQSLLML 437
XP_015791357 455 LLTS--NTKQALREKSAMLDHLENLLRMGNHSILML 488
EFX86398     364 LLNI--NPSQAQREKDATIQHLNDIERLTNQSLQML 397
CAP33080     387 LQKT--DPKEAEGYKPTVLHRLRYIDLRINGTLAML 420
ESO01307     376 MKASttESSKVDQLRKETADGLKTIDVEVKNALTLL 411
1_pfamImport 150 ICMC--DLYECNKIKRLPLLRLRSCCAFLAQTVKIL 183
EEN69130     401 VRET--MPEKTADMKPSLIQHLRVIDERINQSIQLL 434
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