5CVB

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a1a1 of type I collagen

Summary for 5CVB

• Entry DOI: 10.2210/pdb5cvb/pdb
• Descriptor: Collagen alpha-1(I) chain,Collagen alpha-1(IX) chain, Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain, Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain, ... (5 entities in total)
• Functional Keywords: collagen, hetero-trimerization, chain stagger, chain register, triple helix, structural protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Secreted, extracellular space, extracellular matrix : P20849 Q14055 Q14050
• Total number of polymer chains: 6
• Total formula weight: 42525.30

Authors

Boudko, S.P.,Bachinger, H.P. (deposition date: 2015-07-25, release date: 2016-08-10, Last modification date: 2024-11-13)

Primary citation

Boudko, S.P.,Bachinger, H.P.
Structural insight for chain selection and stagger control in collagen.
Sci Rep, 6:37831-37831, 2016

PubMed Abstract: Collagen plays a fundamental role in all known metazoans. In collagens three polypeptides form a unique triple-helical structure with a one-residue stagger to fit every third glycine residue in the inner core without disturbing the poly-proline type II helical conformation of each chain. There are homo- and hetero-trimeric types of collagen consisting of one, two or three distinct chains. Thus there must be mechanisms that control composition and stagger during collagen folding. Here, we uncover the structural basis for both chain selection and stagger formation of a collagen molecule. Three distinct chains (α1, α2 and α3) of the non-collagenous domain 2 (NC2) of type IX collagen are assembled to guide triple-helical sequences in the leading, middle and trailing positions. This unique domain opens the door for generating any fragment of collagen in its native composition and stagger.

PubMed: 27897211
DOI: 10.1038/srep37831

Experimental method

X-RAY DIFFRACTION (2.249 Å)