PDBsum entry 3i84

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protein metals Protein-protein interface(s) links
Cell adhesion PDB id
Protein chains
79 a.a. *
85 a.a. *
Waters ×160
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: The crystal structure of human emmprin n-terminal domain 1 in p6(1)22 space group
Structure: Cervical emmprin. Chain: a, b. Fragment: residues 13-103. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_organ: kidney.
2.00Å     R-factor:   0.189     R-free:   0.207
Authors: J.Luo,G.L.Gilliland
Key ref:
J.Luo et al. (2009). Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-strand swapping. Proteins, 77, 1009-1014. PubMed id: 19768682 DOI: 10.1002/prot.22577
09-Jul-09     Release date:   06-Oct-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P35613  (BASI_HUMAN) -  Basigin
385 a.a.
79 a.a.*
Protein chain
Pfam   ArchSchema ?
P35613  (BASI_HUMAN) -  Basigin
385 a.a.
85 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 


DOI no: 10.1002/prot.22577 Proteins 77:1009-1014 (2009)
PubMed id: 19768682  
Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-strand swapping.
J.Luo, A.Teplyakov, G.Obmolova, T.Malia, S.J.Wu, E.Beil, A.Baker, B.Swencki-Underwood, Y.Zhao, J.Sprenkle, K.Dixon, R.Sweet, G.L.Gilliland.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. A, Molecular structure of ND1 strand swapped dimer. Molecules A and B of ND1 are colored green and cyan, respectively. The signal sequence segment of Mol B is colored red. B, The N-terminal domain of full length EMMPRIN (PDB ID 3B5H) is overlaid on Mol A and shown in gold. The residues of 58-65 are colored blue in panels A and B. For the un-swapped ND1 of 3B5H, this segment was replaced with the same segment ofthe current ND1 structure. The domain swap hinge P[91]EP[93] is colored magenta on the dimer and unswapped monomer. C, A schematic of -strand swapping of ND1.
Figure 3.
Figure 3. SEC-SLS of elution profiles of ND1 at pH 7.5 and 3.5. The ND1 protein was injected at 1.0 mg/mL onto Superdex-75 in PBS pH 7.5 or in 20 mM sodium citrate pH 3.5, 100 mM NaCl. Results show an average MW 13-16 kDa at pH 7.5 and 11 kDa at pH 3.5 based on static light scattering (SLS). The estimated molecular mass (g/mol) and protein concentration (RI, refractive index in volts) are labeled on the left and right axes, respectively.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 77, 1009-1014) copyright 2009.  
  Figures were selected by an automated process.