Integrin

Integrin alphaVbeta3 extracellular domains
Structure of the extracellular segment of integrin alpha Vbeta3.[1]
Identifiers
SymbolIntegrin_alphaVbeta3
PfamPF08441
Pfam clanCL0159
InterProIPR013649
SCOP21jv2 / SCOPe / SUPFAM
OPM superfamily176
OPM protein2knc
Membranome13
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Integrin alpha cytoplasmic region
Structure of chaperone protein PAPD.[2]
Identifiers
SymbolIntegrin_alpha
PfamPF00357
InterProIPR000413
PROSITEPDOC00215
SCOP21dpk / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Integrin, beta chain (vWA)
Identifiers
SymbolIntegrin_beta
PfamPF00362
InterProIPR002369
SMARTSM00187
PROSITEPDOC00216
SCOP21jv2 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1jv2​, 1kup​, 1kuz​, 1l3y​, 1l5g​, 1m1x​, 1m8o​, 1s4x​, 1txv​, 1ty3​, 1ty5​, 1ty6​, 1ty7​, 1tye​, 1u8c
Integrin beta 7 cytoplasmic domain: complex with filamin
crystal structure of the filamin a repeat 21 complexed with the integrin beta7 cytoplasmic tail peptide
Identifiers
SymbolIntegrin_b_cyt
PfamPF08725
InterProIPR014836
SCOP21m8O / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Integrins are transmembrane receptors that help cell–cell and cell–extracellular matrix (ECM) adhesion.[3] Upon ligand binding, integrins activate signal transduction pathways that mediate cellular signals such as regulation of the cell cycle, organization of the intracellular cytoskeleton, and movement of new receptors to the cell membrane.[4] The presence of integrins allows rapid and flexible responses to events at the cell surface (e.g. signal platelets to initiate an interaction with coagulation factors).

Several types of integrins exist, and one cell generally has multiple different types on its surface. Integrins are found in all animals while integrin-like receptors are found in plant cells.[3]

Integrins work alongside other proteins such as cadherins, the immunoglobulin superfamily cell adhesion molecules, selectins and syndecans, to mediate cell–cell and cell–matrix interaction. Ligands for integrins include fibronectin, vitronectin, collagen and laminin.

  1. ^ Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, Joachimiak A, Goodman SL, Arnaout MA (October 2001). "Crystal structure of the extracellular segment of integrin alpha Vbeta3". Science. 294 (5541): 339–45. Bibcode:2001Sci...294..339X. doi:10.1126/science.1064535. PMC 2885948. PMID 11546839.
  2. ^ Sauer FG, Fütterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G (August 1999). "Structural basis of chaperone function and pilus biogenesis". Science. 285 (5430): 1058–61. doi:10.1126/science.285.5430.1058. PMID 10446050.
  3. ^ a b Hynes RO (September 2002). "Integrins: bidirectional, allosteric signaling machines". Cell. 110 (6): 673–87. doi:10.1016/s0092-8674(02)00971-6. PMID 12297042. S2CID 30326350.
  4. ^ Giancotti FG, Ruoslahti E (August 1999). "Integrin signaling". Science. 285 (5430): 1028–32. doi:10.1126/science.285.5430.1028. PMID 10446041.