From crystal clear ligand binding to designer I domains.
A long awaited crystal structure of an integrin I domain in complex with a peptide derived from collagen has revealed the ligand-bound conformation of this domain and suggests a mechanism for allosteric control of integrin function by ligand binding. Also, a computational protein design approach has allowed the creation of stable, high affinity forms of the I domain for the first time.
B
B
Leitinger
N
N
Hogg
D000494:Allosteric Regulation; D003094:Collagen / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D006801:Humans; D016023:Integrins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D015202:Protein Engineering; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D016023:Integrins; D003094:Collagen