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PDBsum entry 4oi9

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protein ligands links
Cell adhesion PDB id
4oi9

 

 

 

 

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Contents
Protein chain
378 a.a.
Ligands
NAG-NAG ×3
NAG-NAG-BMA-MAN
NAG ×5
EDO ×31
Waters ×97
PDB id:
4oi9
Name: Cell adhesion
Title: Crystal structure of icam-5 d1-d4 ectodomain fragment, space group p21
Structure: Intercellular adhesion molecule 5. Chain: a. Fragment: d1-d4. Synonym: icam-5, telencephalin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: icam5, tlcn, tln. Expressed in: homo sapiens. Expression_system_taxid: 9606
Resolution:
2.50Å     R-factor:   0.251     R-free:   0.263
Authors: R.Recacha,D.Jimenez,L.Tian,R.Barredo,C.Ghamberg,J.M.Casasnovas
Key ref: R.Recacha et al. (2014). Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions. Acta Crystallogr D Biol Crystallogr, 70, 1934-1943. PubMed id: 25004970 DOI: 10.1107/S1399004714009468
Date:
19-Jan-14     Release date:   16-Jul-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UMF0  (ICAM5_HUMAN) -  Intercellular adhesion molecule 5 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
924 a.a.
378 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1107/S1399004714009468 Acta Crystallogr D Biol Crystallogr 70:1934-1943 (2014)
PubMed id: 25004970  
 
 
Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions.
R.Recacha, D.Jiménez, L.Tian, R.Barredo, C.G.Gahmberg, J.M.Casasnovas.
 
  ABSTRACT  
 
Intercellular cell adhesion molecule-5 (ICAM-5) is a member of the ICAM subfamily that is exclusively expressed in the telencephalon region of the brain. The crystal structure of the four most N-terminal glycosylated domains (D1-D4) of ICAM-5 was determined in three different space groups and the D1-D5 fragment was modelled. The structures showed a curved molecule with two pronounced interdomain bends between D2 and D3 and between D3 and D4, as well as some interdomain flexibility. In contrast to ICAM-1, ICAM-5 has patches of positive and negative electrostatic charge at D1-D2 and at D3-D5, respectively. ICAM-5 can mediate homotypic interactions. In the crystals, several charge-based intermolecular interactions between the N-terminal and C-terminal moieties of the ICAM-5 molecules were observed, which defined an interacting surface in the D1-D4 fragment. One of the crystal lattices has a molecular assembly that could represent the homophilic ICAM-5 cell adhesion complex in neurons.
 

 

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